Iron in PDB 3zom: M.Acetivorans Protoglobin F145W Mutant

The structure of M.Acetivorans Protoglobin F145W Mutant, PDB code: 3zom was solved by L.Tilleman, S.Abbruzzetti, C.Ciaccio, G.De Sanctis, M.Nardini, A.Pesce, F.Desmet, L.Moens, S.Van Doorslaer, S.Bruno, M.Bolognesi, P.Ascenzi, M.Coletta, C.Viappiani, S.Dewilde, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	80.58 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	50.974, 48.147, 81.001, 90.00, 95.06, 90.00
R / Rfree (%)	18.8 / 23.29

The binding sites of Iron atom in the M.Acetivorans Protoglobin F145W Mutant (pdb code 3zom). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the M.Acetivorans Protoglobin F145W Mutant, PDB code: 3zom:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the M.Acetivorans Protoglobin F145W Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of M.Acetivorans Protoglobin F145W Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe200 b:10.6 occ:1.00 FE A:HEM200 0.0 10.6 1.0 NC A:HEM200 2.0 11.2 1.0 NA A:HEM200 2.0 10.7 1.0 NB A:HEM200 2.1 9.5 1.0 NE2 A:HIS120 2.1 9.2 1.0 ND A:HEM200 2.1 10.7 1.0 CE1 A:HIS120 3.0 10.4 1.0 C4C A:HEM200 3.0 11.6 1.0 C1C A:HEM200 3.0 11.7 1.0 C4A A:HEM200 3.0 11.7 1.0 C1A A:HEM200 3.0 10.8 1.0 C4D A:HEM200 3.1 10.7 1.0 C1B A:HEM200 3.1 8.3 1.0 C1D A:HEM200 3.1 10.9 1.0 C4B A:HEM200 3.1 9.2 1.0 CD2 A:HIS120 3.1 9.6 1.0 CHD A:HEM200 3.4 9.3 1.0 CHA A:HEM200 3.4 9.8 1.0 CHB A:HEM200 3.4 10.0 1.0 CHC A:HEM200 3.4 9.6 1.0 CE2 A:PHE93 4.1 17.5 1.0 ND1 A:HIS120 4.1 9.5 1.0 C3C A:HEM200 4.2 10.1 1.0 CG A:HIS120 4.2 10.7 1.0 C2C A:HEM200 4.2 11.3 1.0 C3A A:HEM200 4.2 12.1 1.0 C2A A:HEM200 4.2 11.8 1.0 C3D A:HEM200 4.3 11.7 1.0 C2D A:HEM200 4.3 11.3 1.0 C2B A:HEM200 4.3 8.2 1.0 C3B A:HEM200 4.3 6.8 1.0 CZ A:PHE93 4.6 19.2 1.0 CD2 A:PHE93 4.7 17.1 1.0 CZ3 A:TRP145 4.7 17.2 1.0

Iron binding site 2 out of 2 in the M.Acetivorans Protoglobin F145W Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of M.Acetivorans Protoglobin F145W Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe200 b:10.3 occ:1.00 FE B:HEM200 0.0 10.3 1.0 NC B:HEM200 2.0 11.4 1.0 NA B:HEM200 2.0 10.1 1.0 NB B:HEM200 2.1 9.3 1.0 ND B:HEM200 2.1 10.8 1.0 NE2 B:HIS120 2.2 8.9 1.0 C4C B:HEM200 3.0 11.0 1.0 C4A B:HEM200 3.0 11.2 1.0 C1C B:HEM200 3.0 11.6 1.0 C1A B:HEM200 3.0 10.9 1.0 C1B B:HEM200 3.0 7.4 1.0 C4D B:HEM200 3.1 10.0 1.0 C4B B:HEM200 3.1 9.8 1.0 C1D B:HEM200 3.1 11.1 1.0 CD2 B:HIS120 3.1 7.1 1.0 CE1 B:HIS120 3.3 8.3 1.0 CHB B:HEM200 3.4 9.1 1.0 CHD B:HEM200 3.4 9.4 1.0 CHA B:HEM200 3.4 9.3 1.0 CHC B:HEM200 3.4 11.0 1.0 CE2 B:PHE93 3.9 19.2 1.0 C3C B:HEM200 4.2 9.2 1.0 C2C B:HEM200 4.2 10.9 1.0 C3A B:HEM200 4.2 12.0 1.0 C2A B:HEM200 4.2 11.8 1.0 C2B B:HEM200 4.3 7.8 1.0 C3D B:HEM200 4.3 10.9 1.0 CG B:HIS120 4.3 10.5 1.0 C3B B:HEM200 4.3 7.4 1.0 C2D B:HEM200 4.3 10.9 1.0 ND1 B:HIS120 4.3 9.4 1.0 CZ B:PHE93 4.4 19.0 1.0 CD2 B:PHE93 4.6 19.1 1.0 CZ3 B:TRP145 4.7 17.7 1.0

L.Tilleman, S.Abbruzzetti, C.Ciaccio, G.De Sanctis, M.Nardini, A.Pesce, F.Desmet, L.Moens, S.Van Doorslaer, S.Bruno, M.Bolognesi, P.Ascenzi, M.Coletta, C.Viappiani, S.Dewilde. Structural Bases For the Regulation of Co Binding in the Archaeal Protoglobin From Methanosarcina Acetivorans To Be Published.