Atomistry » Iron » PDB 1mpy-1n5u » 1mqf
Atomistry »
  Iron »
    PDB 1mpy-1n5u »
      1mqf »

Iron in PDB 1mqf: Compound I From Proteus Mirabilis Catalase

Enzymatic activity of Compound I From Proteus Mirabilis Catalase

All present enzymatic activity of Compound I From Proteus Mirabilis Catalase:
1.11.1.6;

Protein crystallography data

The structure of Compound I From Proteus Mirabilis Catalase, PDB code: 1mqf was solved by P.Andreoletti, A.Pernoud, G.Sainz, P.Gouet, H.M.Jouve, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.96 / 2.50
Space group P 62 2 2
Cell size a, b, c (Å), α, β, γ (°) 110.000, 110.000, 250.000, 90.00, 90.00, 120.00
R / Rfree (%) 19.6 / 23.4

Iron Binding Sites:

The binding sites of Iron atom in the Compound I From Proteus Mirabilis Catalase (pdb code 1mqf). 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 Compound I From Proteus Mirabilis Catalase, PDB code: 1mqf:

Iron binding site 1 out of 1 in 1mqf

Go back to Iron Binding Sites List in 1mqf
Iron binding site 1 out of 1 in the Compound I From Proteus Mirabilis Catalase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Compound I From Proteus Mirabilis Catalase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:23.7
occ:1.00
FE A:HEM501 0.0 23.7 1.0
O A:O500 1.8 28.2 1.0
ND A:HEM501 2.0 20.9 1.0
NB A:HEM501 2.0 20.7 1.0
NC A:HEM501 2.0 21.6 1.0
NA A:HEM501 2.1 21.6 1.0
OH A:TYR337 2.1 26.8 1.0
C4B A:HEM501 3.0 21.5 1.0
C4D A:HEM501 3.0 21.5 1.0
C1D A:HEM501 3.0 21.2 1.0
C1B A:HEM501 3.0 22.4 1.0
C1C A:HEM501 3.1 21.2 1.0
C1A A:HEM501 3.1 21.4 1.0
CZ A:TYR337 3.1 25.8 1.0
C4C A:HEM501 3.1 20.9 1.0
C4A A:HEM501 3.1 21.6 1.0
CHC A:HEM501 3.3 21.2 1.0
CHA A:HEM501 3.4 21.6 1.0
CHD A:HEM501 3.4 19.7 1.0
CHB A:HEM501 3.4 22.7 1.0
CE1 A:TYR337 3.8 25.2 1.0
CE2 A:TYR337 3.9 24.2 1.0
NH2 A:ARG333 4.1 23.7 1.0
C3D A:HEM501 4.2 19.5 1.0
C3B A:HEM501 4.2 21.1 1.0
C2D A:HEM501 4.3 19.3 1.0
C2B A:HEM501 4.3 20.4 1.0
NE A:ARG333 4.3 24.9 1.0
O A:HOH695 4.3 37.0 1.0
C2C A:HEM501 4.3 22.0 1.0
C2A A:HEM501 4.3 21.5 1.0
C3C A:HEM501 4.3 20.9 1.0
C3A A:HEM501 4.4 20.9 1.0
CZ A:PHE140 4.4 20.6 1.0
CZ A:ARG333 4.6 25.2 1.0
NE2 A:HIS54 4.7 24.3 1.0
CD2 A:HIS54 4.8 21.5 1.0
CE2 A:PHE140 5.0 19.8 1.0

Reference:

P.Andreoletti, A.Pernoud, G.Sainz, P.Gouet, H.M.Jouve. Structural Studies of Proteus Mirabilis Catalase in Its Ground State, Oxidized State and in Complex with Formic Acid. Acta Crystallogr.,Sect.D V. 59 2163 2003.
ISSN: ISSN 0907-4449
PubMed: 14646074
DOI: 10.1107/S0907444903019620
Page generated: Wed Jul 16 18:17:43 2025

Last articles

Fe in 2FCV
Fe in 2FCT
Fe in 2FC2
Fe in 2FC1
Fe in 2FBZ
Fe in 2FAL
Fe in 2FAM
Fe in 2EWK
Fe in 2EWI
Fe in 2EWU
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy