Iron in PDB 2jh3: The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains

The structure of The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains, PDB code: 2jh3 was solved by H.-K.S.Leiros, S.M.Mcsweeney, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.9
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	124.780, 128.690, 135.080, 90.00, 90.00, 90.00
R / Rfree (%)	18.9 / 23.8

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 16;

Binding sites:

The binding sites of Iron atom in the The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains (pdb code 2jh3). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 16 binding sites of Iron where determined in the The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains, PDB code: 2jh3:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 16 in the The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe650 b:17.3 occ:1.00 FE1 A:SF4650 0.0 17.3 1.0 SG A:CYS448 2.3 18.2 1.0 S2 A:SF4650 2.3 18.0 1.0 S3 A:SF4650 2.3 17.3 1.0 S4 A:SF4650 2.4 19.0 1.0 FE3 A:SF4650 2.7 17.8 1.0 FE2 A:SF4650 2.7 19.2 1.0 FE4 A:SF4650 2.7 19.4 1.0 CB A:CYS448 3.2 16.4 1.0 S1 A:SF4650 3.9 16.8 1.0 O A:GLU450 4.1 16.6 1.0 NE1 A:TRP429 4.2 21.0 1.0 CA A:CYS448 4.5 17.4 1.0 CD A:ARG425 4.7 17.9 1.0 SG A:CYS423 4.7 15.2 1.0 CB A:ARG425 4.7 16.2 1.0 SG A:CYS452 4.8 18.1 1.0 N A:CYS452 4.8 19.6 1.0 O A:HOH2288 4.8 39.0 1.0 SG A:CYS420 4.8 19.6 1.0 CB A:CYS452 4.9 19.6 1.0 C A:GLU450 5.0 17.9 1.0

Iron binding site 2 out of 16 in the The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe650 b:19.2 occ:1.00 FE2 A:SF4650 0.0 19.2 1.0 S1 A:SF4650 2.3 16.8 1.0 S4 A:SF4650 2.3 19.0 1.0 S3 A:SF4650 2.3 17.3 1.0 SG A:CYS452 2.4 18.1 1.0 FE3 A:SF4650 2.7 17.8 1.0 FE1 A:SF4650 2.7 17.3 1.0 FE4 A:SF4650 2.7 19.4 1.0 CB A:CYS452 3.2 19.6 1.0 S2 A:SF4650 3.9 18.0 1.0 N A:CYS452 4.0 19.6 1.0 CA A:CYS452 4.2 20.1 1.0 CB A:LEU455 4.7 19.3 1.0 SG A:CYS448 4.8 18.2 1.0 CG2 A:ILE343 4.8 20.8 1.0 SG A:CYS423 4.8 15.2 1.0 SG A:CYS420 4.9 19.6 1.0 NE1 A:TRP346 5.0 18.9 1.0

Iron binding site 3 out of 16 in the The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe650 b:17.8 occ:1.00 FE3 A:SF4650 0.0 17.8 1.0 SG A:CYS423 2.3 15.2 1.0 S4 A:SF4650 2.3 19.0 1.0 S1 A:SF4650 2.3 16.8 1.0 S2 A:SF4650 2.3 18.0 1.0 FE1 A:SF4650 2.7 17.3 1.0 FE2 A:SF4650 2.7 19.2 1.0 FE4 A:SF4650 2.7 19.4 1.0 CB A:CYS423 3.1 16.2 1.0 S3 A:SF4650 3.9 17.3 1.0 CB A:ARG425 4.2 16.2 1.0 NE1 A:TRP346 4.3 18.9 1.0 CD A:ARG425 4.5 17.9 1.0 CA A:CYS423 4.6 16.1 1.0 OG1 A:THR345 4.6 14.7 1.0 CG2 A:ILE343 4.6 20.8 1.0 SG A:CYS448 4.7 18.2 1.0 CG A:ARG425 4.7 15.0 1.0 CD1 A:TRP346 4.8 17.2 1.0 SG A:CYS420 4.9 19.6 1.0 SG A:CYS452 4.9 18.1 1.0 CB A:CYS448 4.9 16.4 1.0

Iron binding site 4 out of 16 in the The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe650 b:19.4 occ:1.00 FE4 A:SF4650 0.0 19.4 1.0 S2 A:SF4650 2.3 18.0 1.0 S3 A:SF4650 2.3 17.3 1.0 S1 A:SF4650 2.3 16.8 1.0 SG A:CYS420 2.4 19.6 1.0 FE2 A:SF4650 2.7 19.2 1.0 FE1 A:SF4650 2.7 17.3 1.0 FE3 A:SF4650 2.7 17.8 1.0 CB A:CYS420 3.3 18.6 1.0 CA A:CYS420 3.8 19.3 1.0 S4 A:SF4650 4.0 19.0 1.0 N A:CYS420 4.5 18.1 1.0 CB A:CYS423 4.6 16.2 1.0 CD2 A:LEU455 4.6 19.9 1.0 SG A:CYS423 4.7 15.2 1.0 SG A:CYS448 4.8 18.2 1.0 SG A:CYS452 4.8 18.1 1.0 O A:HOH2267 5.0 35.8 1.0

Iron binding site 5 out of 16 in the The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe650 b:20.1 occ:1.00 FE1 B:SF4650 0.0 20.1 1.0 SG B:CYS448 2.3 19.5 1.0 S2 B:SF4650 2.3 21.7 1.0 S3 B:SF4650 2.3 20.1 1.0 S4 B:SF4650 2.3 19.4 1.0 FE4 B:SF4650 2.7 19.6 1.0 FE3 B:SF4650 2.7 21.9 1.0 FE2 B:SF4650 2.8 20.7 1.0 CB B:CYS448 3.3 18.9 1.0 S1 B:SF4650 3.9 19.2 1.0 O B:GLU450 4.0 20.6 1.0 NE1 B:TRP429 4.5 21.0 1.0 CA B:CYS448 4.6 18.4 1.0 CD B:ARG425 4.7 18.1 1.0 SG B:CYS423 4.8 17.9 1.0 SG B:CYS452 4.8 22.5 1.0 CB B:CYS452 4.8 22.8 1.0 CB B:ARG425 4.9 18.9 1.0 SG B:CYS420 4.9 23.6 1.0 N B:CYS452 4.9 22.6 1.0 C B:GLU450 4.9 21.8 1.0 O B:HOH2176 5.0 42.0 1.0

Iron binding site 6 out of 16 in the The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe650 b:20.7 occ:1.00 FE2 B:SF4650 0.0 20.7 1.0 S1 B:SF4650 2.3 19.2 1.0 S3 B:SF4650 2.3 20.1 1.0 SG B:CYS452 2.3 22.5 1.0 S4 B:SF4650 2.4 19.4 1.0 FE3 B:SF4650 2.7 21.9 1.0 FE1 B:SF4650 2.8 20.1 1.0 FE4 B:SF4650 2.8 19.6 1.0 CB B:CYS452 3.2 22.8 1.0 S2 B:SF4650 3.9 21.7 1.0 N B:CYS452 4.1 22.6 1.0 CA B:CYS452 4.2 23.1 1.0 CB B:LEU455 4.5 24.9 1.0 CG2 B:ILE343 4.7 19.7 1.0 SG B:CYS420 4.8 23.6 1.0 SG B:CYS448 4.8 19.5 1.0 SG B:CYS423 4.9 17.9 1.0 N B:LEU455 5.0 24.2 1.0 CG1 B:ILE343 5.0 20.5 1.0 NE1 B:TRP346 5.0 20.4 1.0 CD1 B:ILE343 5.0 21.0 1.0

Iron binding site 7 out of 16 in the The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe650 b:21.9 occ:1.00 FE3 B:SF4650 0.0 21.9 1.0 S4 B:SF4650 2.3 19.4 1.0 S2 B:SF4650 2.3 21.7 1.0 S1 B:SF4650 2.3 19.2 1.0 SG B:CYS420 2.4 23.6 1.0 FE2 B:SF4650 2.7 20.7 1.0 FE4 B:SF4650 2.7 19.6 1.0 FE1 B:SF4650 2.7 20.1 1.0 CB B:CYS420 3.2 23.6 1.0 CA B:CYS420 3.8 23.2 1.0 S3 B:SF4650 3.9 20.1 1.0 N B:CYS420 4.5 24.6 1.0 CB B:CYS423 4.6 20.7 1.0 CD2 B:LEU455 4.7 26.4 1.0 SG B:CYS423 4.7 17.9 1.0 SG B:CYS448 4.8 19.5 1.0 SG B:CYS452 4.8 22.5 1.0 CB B:LEU455 4.9 24.9 1.0 CD B:ARG427 4.9 29.2 1.0 O B:HOH2163 4.9 38.2 1.0 C B:CYS420 5.0 24.1 1.0

Iron binding site 8 out of 16 in the The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe650 b:19.6 occ:1.00 FE4 B:SF4650 0.0 19.6 1.0 S3 B:SF4650 2.3 20.1 1.0 S1 B:SF4650 2.3 19.2 1.0 S2 B:SF4650 2.3 21.7 1.0 SG B:CYS423 2.3 17.9 1.0 FE1 B:SF4650 2.7 20.1 1.0 FE3 B:SF4650 2.7 21.9 1.0 FE2 B:SF4650 2.8 20.7 1.0 CB B:CYS423 3.1 20.7 1.0 S4 B:SF4650 3.9 19.4 1.0 CB B:ARG425 4.4 18.9 1.0 CD B:ARG425 4.4 18.1 1.0 NE1 B:TRP346 4.4 20.4 1.0 OG1 B:THR345 4.5 19.6 1.0 CA B:CYS423 4.5 20.2 1.0 CG2 B:ILE343 4.6 19.7 1.0 SG B:CYS448 4.7 19.5 1.0 CD1 B:TRP346 4.7 20.4 1.0 CG B:ARG425 4.8 18.5 1.0 SG B:CYS420 4.8 23.6 1.0 CB B:CYS420 4.9 23.6 1.0 SG B:CYS452 4.9 22.5 1.0 CA B:CYS420 5.0 23.2 1.0

Iron binding site 9 out of 16 in the The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe650 b:18.5 occ:1.00 FE1 C:SF4650 0.0 18.5 1.0 SG C:CYS448 2.3 21.3 1.0 S2 C:SF4650 2.3 17.5 1.0 S3 C:SF4650 2.3 21.2 1.0 S4 C:SF4650 2.3 19.5 1.0 FE3 C:SF4650 2.7 19.3 1.0 FE2 C:SF4650 2.7 18.0 1.0 FE4 C:SF4650 2.7 21.6 1.0 CB C:CYS448 3.3 19.9 1.0 S1 C:SF4650 3.9 17.4 1.0 O C:GLU450 4.1 22.2 1.0 NE1 C:TRP429 4.2 27.0 1.0 CD C:ARG425 4.5 17.7 1.0 CA C:CYS448 4.6 20.2 1.0 SG C:CYS423 4.7 17.0 1.0 CB C:CYS452 4.7 20.5 1.0 CB C:ARG425 4.8 17.0 1.0 SG C:CYS452 4.8 18.4 1.0 N C:CYS452 4.8 21.2 1.0 SG C:CYS420 4.8 25.8 1.0 C C:GLU450 4.9 21.3 1.0 O C:HOH2278 5.0 37.5 1.0

Iron binding site 10 out of 16 in the The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi-Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe650 b:18.0 occ:1.00 FE2 C:SF4650 0.0 18.0 1.0 SG C:CYS423 2.3 17.0 1.0 S4 C:SF4650 2.3 19.5 1.0 S3 C:SF4650 2.4 21.2 1.0 S1 C:SF4650 2.4 17.4 1.0 FE3 C:SF4650 2.7 19.3 1.0 FE1 C:SF4650 2.7 18.5 1.0 FE4 C:SF4650 2.7 21.6 1.0 CB C:CYS423 3.1 15.3 1.0 S2 C:SF4650 3.9 17.5 1.0 CB C:ARG425 4.3 17.0 1.0 NE1 C:TRP346 4.4 16.2 1.0 CD C:ARG425 4.4 17.7 1.0 CG2 C:ILE343 4.5 17.7 1.0 OG1 C:THR345 4.6 19.2 1.0 CA C:CYS423 4.6 18.2 1.0 SG C:CYS448 4.7 21.3 1.0 CG C:ARG425 4.7 16.8 1.0 CD1 C:TRP346 4.7 16.1 1.0 SG C:CYS420 4.9 25.8 1.0 SG C:CYS452 4.9 18.4 1.0 CB C:CYS420 4.9 23.0 1.0

H.-K.S.Leiros, S.M.Mcsweeney. The Crystal Structure of DR2241 From Deinococcus Radiodurans at 1.9 A Resolution Reveals A Multi- Domain Protein with Structural Similarity to Chelatases But Also with Two Additional Novel Domains J.Struct.Biol. V. 159 92 2007.
ISSN: ISSN 1047-8477
PubMed: 17448684
DOI: 10.1016/J.JSB.2007.02.009