Iron in PDB 2mhm: Solution Structure of Cytochrome C Y67H

The binding sites of Iron atom in the Solution Structure of Cytochrome C Y67H (pdb code 2mhm). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Solution Structure of Cytochrome C Y67H, PDB code: 2mhm:

Iron binding site 1 out of 1 in the Solution Structure of Cytochrome C Y67H


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Solution Structure of Cytochrome C Y67H within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:0.0 occ:1.00 FE A:HEC201 0.0 0.0 1.0 NC A:HEC201 2.0 0.0 1.0 ND A:HEC201 2.0 0.0 1.0 NA A:HEC201 2.0 0.0 1.0 NB A:HEC201 2.0 0.0 1.0 NE2 A:HIS18 2.1 0.0 1.0 SD A:MET80 2.4 0.0 1.0 C1C A:HEC201 3.0 0.0 1.0 C4A A:HEC201 3.0 0.0 1.0 C1D A:HEC201 3.0 0.0 1.0 C4B A:HEC201 3.0 0.0 1.0 C4D A:HEC201 3.0 0.0 1.0 C1B A:HEC201 3.0 0.0 1.0 C4C A:HEC201 3.0 0.0 1.0 C1A A:HEC201 3.0 0.0 1.0 CD2 A:HIS18 3.1 0.0 1.0 CE1 A:HIS18 3.2 0.0 1.0 HD2 A:HIS18 3.2 0.0 1.0 CHC A:HEC201 3.4 0.0 1.0 CHB A:HEC201 3.4 0.0 1.0 CHD A:HEC201 3.4 0.0 1.0 CHA A:HEC201 3.4 0.0 1.0 HE1 A:HIS18 3.4 0.0 1.0 HG3 A:MET80 3.6 0.0 1.0 HE2 A:MET80 3.6 0.0 1.0 CG A:MET80 3.6 0.0 1.0 CE A:MET80 3.7 0.0 1.0 HB2 A:MET80 3.9 0.0 1.0 HE3 A:MET80 4.1 0.0 1.0 C2C A:HEC201 4.2 0.0 1.0 C2D A:HEC201 4.2 0.0 1.0 C3A A:HEC201 4.2 0.0 1.0 C3D A:HEC201 4.2 0.0 1.0 C3C A:HEC201 4.2 0.0 1.0 C2A A:HEC201 4.2 0.0 1.0 C2B A:HEC201 4.3 0.0 1.0 CG A:HIS18 4.3 0.0 1.0 C3B A:HEC201 4.3 0.0 1.0 ND1 A:HIS18 4.3 0.0 1.0 HE2 A:HIS67 4.3 0.0 1.0 CB A:MET80 4.3 0.0 1.0 HHC A:HEC201 4.5 0.0 1.0 HHB A:HEC201 4.5 0.0 1.0 HHD A:HEC201 4.5 0.0 1.0 HHA A:HEC201 4.5 0.0 1.0 HG2 A:MET80 4.5 0.0 1.0 HE1 A:MET80 4.5 0.0 1.0 HA3 A:GLY29 4.7 0.0 1.0 HD2 A:PRO30 4.7 0.0 1.0 HB3 A:MET80 4.9 0.0 1.0 HB3 A:CYS17 4.9 0.0 1.0 HD13 A:LEU32 4.9 0.0 1.0

W.X.Lan, Z.H.Wang, Z.Z.Yang, T.L.Ying, X.Zhang, X.S.Tan, M.Liu, C.Y.Cao, Z.X.Huang. Structural Basis For Cytochrome C Y67H Mutant to Function As A Peroxidase Plos One V. 9 07305 2014.
ISSN: ESSN 1932-6203
PubMed: 25210769
DOI: 10.1371/JOURNAL.PONE.0107305