Iron in PDB 1mqv: Crystal Structure of the Q1A/F32W/W72F Mutant of Rhodopseudomonas Palustris Cytochrome C' (Prime) Expressed in E. Coli

The structure of Crystal Structure of the Q1A/F32W/W72F Mutant of Rhodopseudomonas Palustris Cytochrome C' (Prime) Expressed in E. Coli, PDB code: 1mqv was solved by J.C.Lee, K.C.Engman, F.A.Tezcan, H.B.Gray, J.R.Winkler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.00 / 1.78
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	33.839, 62.085, 113.419, 90.00, 90.00, 90.00
R / Rfree (%)	21.4 / 26.5

The binding sites of Iron atom in the Crystal Structure of the Q1A/F32W/W72F Mutant of Rhodopseudomonas Palustris Cytochrome C' (Prime) Expressed in E. Coli (pdb code 1mqv). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of the Q1A/F32W/W72F Mutant of Rhodopseudomonas Palustris Cytochrome C' (Prime) Expressed in E. Coli, PDB code: 1mqv:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of the Q1A/F32W/W72F Mutant of Rhodopseudomonas Palustris Cytochrome C' (Prime) Expressed in E. Coli


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 Q1A/F32W/W72F Mutant of Rhodopseudomonas Palustris Cytochrome C' (Prime) Expressed in E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe150 b:23.0 occ:1.00 FE A:HEM150 0.0 23.0 1.0 NB A:HEM150 1.9 19.6 1.0 NC A:HEM150 2.0 24.4 1.0 ND A:HEM150 2.0 21.4 1.0 NA A:HEM150 2.1 20.8 1.0 NE2 A:HIS117 2.1 18.5 1.0 C4B A:HEM150 3.0 18.9 1.0 C4D A:HEM150 3.0 32.0 1.0 C1B A:HEM150 3.0 23.2 1.0 C1A A:HEM150 3.0 24.9 1.0 C1C A:HEM150 3.1 22.0 1.0 CE1 A:HIS117 3.1 26.1 1.0 C4A A:HEM150 3.1 18.3 1.0 C4C A:HEM150 3.1 18.5 1.0 C1D A:HEM150 3.1 17.9 1.0 CD2 A:HIS117 3.1 19.0 1.0 CHA A:HEM150 3.4 30.8 1.0 CHC A:HEM150 3.4 25.4 1.0 CHB A:HEM150 3.4 25.4 1.0 CD2 A:LEU12 3.5 20.3 1.0 CHD A:HEM150 3.5 19.8 1.0 ND1 A:HIS117 4.2 24.0 1.0 NH1 A:ARG121 4.2 28.7 1.0 C2A A:HEM150 4.3 19.1 1.0 CG A:HIS117 4.3 23.7 1.0 C3B A:HEM150 4.3 21.3 1.0 C2C A:HEM150 4.3 22.3 1.0 C3D A:HEM150 4.3 15.9 1.0 C2B A:HEM150 4.3 28.2 1.0 C3A A:HEM150 4.3 21.1 1.0 C2D A:HEM150 4.4 25.1 1.0 C3C A:HEM150 4.4 22.4 1.0 CG A:LEU12 4.5 23.5 1.0 CB A:LEU12 4.7 21.5 1.0 CD1 A:LEU12 4.7 28.8 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the Q1A/F32W/W72F Mutant of Rhodopseudomonas Palustris Cytochrome C' (Prime) Expressed in E. Coli


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 Q1A/F32W/W72F Mutant of Rhodopseudomonas Palustris Cytochrome C' (Prime) Expressed in E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe150 b:30.1 occ:1.00 FE B:HEM150 0.0 30.1 1.0 NA B:HEM150 1.9 28.5 1.0 NC B:HEM150 2.0 24.6 1.0 NB B:HEM150 2.0 30.7 1.0 NE2 B:HIS117 2.1 26.1 1.0 ND B:HEM150 2.1 29.0 1.0 C1C B:HEM150 3.0 26.5 1.0 C4B B:HEM150 3.0 36.2 1.0 CE1 B:HIS117 3.0 48.7 1.0 C1A B:HEM150 3.0 35.4 1.0 C4A B:HEM150 3.1 23.4 1.0 C4D B:HEM150 3.1 35.6 1.0 C1D B:HEM150 3.1 24.9 1.0 CD2 B:HIS117 3.1 28.8 1.0 C4C B:HEM150 3.1 24.2 1.0 C1B B:HEM150 3.1 30.6 1.0 CHC B:HEM150 3.3 27.2 1.0 CHA B:HEM150 3.4 33.6 1.0 CHB B:HEM150 3.5 27.5 1.0 CD2 B:LEU12 3.5 22.7 1.0 CHD B:HEM150 3.5 24.9 1.0 ND1 B:HIS117 4.1 33.1 1.0 C2C B:HEM150 4.2 19.2 1.0 CG B:HIS117 4.2 37.8 1.0 C2A B:HEM150 4.3 28.7 1.0 C3A B:HEM150 4.3 33.2 1.0 C3C B:HEM150 4.3 23.8 1.0 C3D B:HEM150 4.3 26.8 1.0 C3B B:HEM150 4.3 25.0 1.0 C2D B:HEM150 4.3 27.2 1.0 C2B B:HEM150 4.4 34.4 1.0 CG B:LEU12 4.6 27.8 1.0 CD1 B:LEU12 4.8 27.9 1.0 NH1 B:ARG121 4.8 45.1 1.0 CB B:LEU12 4.9 28.7 1.0

J.C.Lee, K.C.Engman, F.A.Tezcan, H.B.Gray, J.R.Winkler. Structural Features of Cytochrome C' Folding Intermediates Revealed By Fluorescence Energy-Transfer Kinetics Proc.Natl.Acad.Sci.Usa V. 99 14778 2002.
ISSN: ISSN 0027-8424
PubMed: 12407175
DOI: 10.1073/PNAS.192574099