Iron in PDB 1wef: Catalytic Domain of Muty From Escherichia Coli K20A Mutant

The structure of Catalytic Domain of Muty From Escherichia Coli K20A Mutant, PDB code: 1wef was solved by K.Hitomi, A.S.Arvai, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	17.43 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	83.696, 49.325, 69.680, 90.00, 123.25, 90.00
R / Rfree (%)	20 / 22

The binding sites of Iron atom in the Catalytic Domain of Muty From Escherichia Coli K20A Mutant (pdb code 1wef). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Catalytic Domain of Muty From Escherichia Coli K20A Mutant, PDB code: 1wef:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Catalytic Domain of Muty From Escherichia Coli K20A Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Catalytic Domain of Muty From Escherichia Coli K20A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe300 b:15.2 occ:1.00 FE1 A:SF4300 0.0 15.2 1.0 S2 A:SF4300 2.2 11.8 1.0 S3 A:SF4300 2.3 14.3 1.0 S4 A:SF4300 2.3 13.5 1.0 SG A:CYS202 2.3 13.1 1.0 FE4 A:SF4300 2.7 16.5 1.0 FE3 A:SF4300 2.7 17.0 1.0 FE2 A:SF4300 2.7 15.9 1.0 CB A:CYS202 3.0 15.5 1.0 S1 A:SF4300 3.9 14.7 1.0 CB A:LEU204 4.4 16.3 1.0 CA A:CYS202 4.5 14.4 1.0 N A:GLN205 4.6 18.7 1.0 SG A:CYS192 4.6 16.0 1.0 CA A:CYS199 4.7 15.5 1.0 CB A:CYS192 4.7 15.6 1.0 C A:LEU204 4.8 17.3 1.0 SG A:CYS208 4.8 12.7 1.0 SG A:CYS199 4.9 16.4 1.0 CD1 A:LEU204 5.0 15.6 1.0 CB A:CYS208 5.0 14.1 1.0 N A:LEU204 5.0 14.4 1.0 CA A:GLN205 5.0 20.2 1.0 CA A:LEU204 5.0 15.9 1.0

Iron binding site 2 out of 4 in the Catalytic Domain of Muty From Escherichia Coli K20A Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Catalytic Domain of Muty From Escherichia Coli K20A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe300 b:15.9 occ:1.00 FE2 A:SF4300 0.0 15.9 1.0 SG A:CYS192 2.2 16.0 1.0 S3 A:SF4300 2.2 14.3 1.0 S1 A:SF4300 2.3 14.7 1.0 S4 A:SF4300 2.3 13.5 1.0 FE1 A:SF4300 2.7 15.2 1.0 FE3 A:SF4300 2.8 17.0 1.0 FE4 A:SF4300 2.8 16.5 1.0 CB A:CYS192 3.1 15.6 1.0 CA A:CYS192 3.8 15.7 1.0 S2 A:SF4300 3.9 11.8 1.0 CD A:ARG147 4.1 14.6 1.0 CB A:PRO197 4.3 18.5 1.0 CB A:ARG147 4.5 13.2 1.0 NH1 A:ARG147 4.6 15.0 1.0 SG A:CYS202 4.8 13.1 1.0 N A:CYS192 4.8 16.0 1.0 SG A:CYS208 4.9 12.7 1.0 CG A:PRO197 4.9 19.2 1.0 C A:CYS192 4.9 17.0 1.0 SG A:CYS199 4.9 16.4 1.0 CG A:ARG147 4.9 13.4 1.0

Iron binding site 3 out of 4 in the Catalytic Domain of Muty From Escherichia Coli K20A Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Catalytic Domain of Muty From Escherichia Coli K20A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe300 b:17.0 occ:1.00 FE3 A:SF4300 0.0 17.0 1.0 S4 A:SF4300 2.2 13.5 1.0 S2 A:SF4300 2.3 11.8 1.0 S1 A:SF4300 2.3 14.7 1.0 SG A:CYS199 2.4 16.4 1.0 FE4 A:SF4300 2.7 16.5 1.0 FE1 A:SF4300 2.7 15.2 1.0 FE2 A:SF4300 2.8 15.9 1.0 CB A:CYS199 3.2 16.6 1.0 CA A:CYS199 3.5 15.5 1.0 S3 A:SF4300 3.7 14.3 1.0 N A:CYS199 4.1 14.8 1.0 CB A:PRO197 4.3 18.5 1.0 CB A:ALA211 4.4 16.9 1.0 CG A:PRO197 4.4 19.2 1.0 CB A:CYS202 4.6 15.5 1.0 SG A:CYS208 4.6 12.7 1.0 SG A:CYS192 4.8 16.0 1.0 SG A:CYS202 4.8 13.1 1.0 C A:CYS199 4.8 16.6 1.0 C A:LYS198 4.9 15.5 1.0

Iron binding site 4 out of 4 in the Catalytic Domain of Muty From Escherichia Coli K20A Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Catalytic Domain of Muty From Escherichia Coli K20A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe300 b:16.5 occ:1.00 FE4 A:SF4300 0.0 16.5 1.0 S3 A:SF4300 2.2 14.3 1.0 S2 A:SF4300 2.3 11.8 1.0 SG A:CYS208 2.3 12.7 1.0 S1 A:SF4300 2.3 14.7 1.0 FE3 A:SF4300 2.7 17.0 1.0 FE1 A:SF4300 2.7 15.2 1.0 FE2 A:SF4300 2.8 15.9 1.0 CB A:CYS208 3.2 14.1 1.0 S4 A:SF4300 3.8 13.5 1.0 SG A:CYS148 4.3 17.5 0.5 CB A:ALA211 4.3 16.9 1.0 CB A:ARG147 4.5 13.2 1.0 N A:ALA211 4.5 17.2 1.0 CA A:CYS208 4.6 16.3 1.0 SG A:CYS192 4.7 16.0 1.0 SG A:CYS199 4.7 16.4 1.0 N A:CYS148 4.8 14.0 0.5 N A:CYS148 4.8 14.1 0.5 CB A:ALA210 4.8 16.9 1.0 SG A:CYS202 4.9 13.1 1.0 CA A:ALA211 5.0 18.1 1.0 CA A:CYS148 5.0 14.4 0.5 CA A:CYS148 5.0 14.3 0.5 C A:ARG147 5.0 13.5 1.0

R.C.Manuel, K.Hitomi, A.S.Arvai, P.G.House, A.J.Kurtz, M.L.Dodson, A.K.Mccullough, J.A.Tainer, R.S.Lloyd. Reaction Intermediates in the Catalytic Mechanism of Escherichia Coli Muty Dna Glycosylase J.Biol.Chem. V. 279 46930 2004.
ISSN: ISSN 0021-9258
PubMed: 15326180
DOI: 10.1074/JBC.M403944200