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Iron in PDB 1xd8: Crystal Structure of the Nitrogenase Fe Protein ASP39ASN

Enzymatic activity of Crystal Structure of the Nitrogenase Fe Protein ASP39ASN

All present enzymatic activity of Crystal Structure of the Nitrogenase Fe Protein ASP39ASN:
1.18.6.1;

Protein crystallography data

The structure of Crystal Structure of the Nitrogenase Fe Protein ASP39ASN, PDB code: 1xd8 was solved by S.B.Jang, M.S.Jeong, L.C.Seefeldt, J.W.Peters, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 57.235, 92.109, 62.821, 90.00, 101.05, 90.00
R / Rfree (%) 22.3 / 29.6

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Nitrogenase Fe Protein ASP39ASN (pdb code 1xd8). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of the Nitrogenase Fe Protein ASP39ASN, PDB code: 1xd8:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1xd8

Go back to Iron Binding Sites List in 1xd8
Iron binding site 1 out of 4 in the Crystal Structure of the Nitrogenase Fe Protein ASP39ASN


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of the Nitrogenase Fe Protein ASP39ASN within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe290

b:42.8
occ:1.00
FE1 A:SF4290 0.0 42.8 1.0
SG B:CYS97 1.9 65.1 1.0
S2 A:SF4290 2.2 45.4 1.0
S4 A:SF4290 2.3 51.8 1.0
S3 A:SF4290 2.4 48.5 1.0
FE4 A:SF4290 2.5 47.6 1.0
FE2 A:SF4290 2.7 45.1 1.0
FE3 A:SF4290 2.7 46.7 1.0
CB B:CYS97 3.3 63.1 1.0
CA B:CYS97 3.6 63.6 1.0
N B:ALA98 3.8 60.6 1.0
CA B:GLY134 3.8 53.4 1.0
S1 A:SF4290 3.9 50.7 1.0
C B:CYS97 4.2 61.7 1.0
N B:GLY134 4.3 54.4 1.0
SG B:CYS132 4.4 48.8 1.0
SG A:CYS97 4.4 55.7 1.0
SG A:CYS132 4.6 49.2 1.0
N B:GLY99 4.7 64.1 1.0
N B:CYS97 4.9 68.9 1.0
CA B:ALA98 5.0 61.4 1.0

Iron binding site 2 out of 4 in 1xd8

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Iron binding site 2 out of 4 in the Crystal Structure of the Nitrogenase Fe Protein ASP39ASN


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of the Nitrogenase Fe Protein ASP39ASN within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe290

b:45.1
occ:1.00
FE2 A:SF4290 0.0 45.1 1.0
SG A:CYS97 1.9 55.7 1.0
S4 A:SF4290 2.2 51.8 1.0
S1 A:SF4290 2.3 50.7 1.0
S3 A:SF4290 2.3 48.5 1.0
FE4 A:SF4290 2.6 47.6 1.0
FE1 A:SF4290 2.7 42.8 1.0
FE3 A:SF4290 2.7 46.7 1.0
CB A:CYS97 3.3 62.2 1.0
CA A:CYS97 3.6 62.6 1.0
N A:ALA98 3.9 60.4 1.0
CA A:GLY134 3.9 51.1 1.0
S2 A:SF4290 3.9 45.4 1.0
C A:CYS97 4.2 59.3 1.0
SG B:CYS97 4.3 65.1 1.0
N A:GLY134 4.4 53.9 1.0
SG A:CYS132 4.4 49.2 1.0
SG B:CYS132 4.7 48.8 1.0
N A:GLY99 4.7 60.1 1.0
N A:CYS97 4.9 73.0 1.0

Iron binding site 3 out of 4 in 1xd8

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Iron binding site 3 out of 4 in the Crystal Structure of the Nitrogenase Fe Protein ASP39ASN


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of the Nitrogenase Fe Protein ASP39ASN within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe290

b:46.7
occ:1.00
FE3 A:SF4290 0.0 46.7 1.0
SG A:CYS132 2.1 49.2 1.0
S2 A:SF4290 2.3 45.4 1.0
S4 A:SF4290 2.3 51.8 1.0
S1 A:SF4290 2.4 50.7 1.0
FE4 A:SF4290 2.6 47.6 1.0
FE2 A:SF4290 2.7 45.1 1.0
FE1 A:SF4290 2.7 42.8 1.0
CB A:CYS132 3.2 48.7 1.0
N A:GLY134 3.9 53.9 1.0
CA A:GLY134 4.0 51.1 1.0
S3 A:SF4290 4.0 48.5 1.0
SG B:CYS97 4.3 65.1 1.0
SG A:CYS97 4.5 55.7 1.0
CA A:CYS132 4.6 52.0 1.0
SG B:CYS132 4.6 48.8 1.0
N B:ALA98 4.6 60.6 1.0
CA B:CYS97 4.7 63.6 1.0
N A:GLY133 4.8 55.2 1.0
C A:CYS132 4.8 54.3 1.0
CD1 A:PHE135 5.0 61.0 1.0
N A:PHE135 5.0 49.7 1.0

Iron binding site 4 out of 4 in 1xd8

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Iron binding site 4 out of 4 in the Crystal Structure of the Nitrogenase Fe Protein ASP39ASN


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of the Nitrogenase Fe Protein ASP39ASN within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe290

b:47.6
occ:1.00
FE4 A:SF4290 0.0 47.6 1.0
SG B:CYS132 2.2 48.8 1.0
S3 A:SF4290 2.3 48.5 1.0
S1 A:SF4290 2.3 50.7 1.0
S2 A:SF4290 2.3 45.4 1.0
FE1 A:SF4290 2.5 42.8 1.0
FE2 A:SF4290 2.6 45.1 1.0
FE3 A:SF4290 2.6 46.7 1.0
CB B:CYS132 3.3 52.3 1.0
S4 A:SF4290 3.7 51.8 1.0
N B:GLY134 3.9 54.4 1.0
CA B:GLY134 3.9 53.4 1.0
SG B:CYS97 4.2 65.1 1.0
SG A:CYS97 4.3 55.7 1.0
SG A:CYS132 4.6 49.2 1.0
CA A:CYS97 4.6 62.6 1.0
N A:ALA98 4.6 60.4 1.0
CA B:CYS132 4.6 52.1 1.0
N B:GLY133 4.8 53.8 1.0
C B:CYS132 4.9 54.5 1.0
CD1 B:PHE135 5.0 68.5 1.0
O A:GLY96 5.0 76.7 1.0
CB A:CYS97 5.0 62.2 1.0
N B:PHE135 5.0 53.4 1.0
C B:GLY134 5.0 54.2 1.0

Reference:

S.B.Jang, M.S.Jeong, L.C.Seefeldt, J.W.Peters. Structural and Biochemical Implications of Single Amino Acid Substitutions in the Nucleotide-Dependent Switch Regions of the Nitrogenase Fe Protein From Azotobacter Vinelandii J.Biol.Inorg.Chem. V. 9 1028 2004.
ISSN: ISSN 0949-8257
PubMed: 15549494
DOI: 10.1007/S00775-004-0605-5
Page generated: Sun Dec 13 14:35:46 2020

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