Atomistry » Iron » PDB 1n5w-1nmi » 1nm0
Atomistry »
  Iron »
    PDB 1n5w-1nmi »
      1nm0 »

Iron in PDB 1nm0: Proteus Mirabilis Catalase in Complex with Formiate

Enzymatic activity of Proteus Mirabilis Catalase in Complex with Formiate

All present enzymatic activity of Proteus Mirabilis Catalase in Complex with Formiate:
1.11.1.6;

Protein crystallography data

The structure of Proteus Mirabilis Catalase in Complex with Formiate, PDB code: 1nm0 was solved by P.Andreoletti, A.Pernoud, P.Gouet, H.M.Jouve, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.98 / 2.30
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 (%) 18.1 / 21.1

Iron Binding Sites:

The binding sites of Iron atom in the Proteus Mirabilis Catalase in Complex with Formiate (pdb code 1nm0). 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 Proteus Mirabilis Catalase in Complex with Formiate, PDB code: 1nm0:

Iron binding site 1 out of 1 in 1nm0

Go back to Iron Binding Sites List in 1nm0
Iron binding site 1 out of 1 in the Proteus Mirabilis Catalase in Complex with Formiate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Proteus Mirabilis Catalase in Complex with Formiate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe491

b:14.6
occ:1.00
FE A:HEM491 0.0 14.6 1.0
ND A:HEM491 1.9 11.9 1.0
NB A:HEM491 2.0 11.3 1.0
NA A:HEM491 2.0 12.0 1.0
OH A:TYR337 2.0 13.8 1.0
NC A:HEM491 2.0 12.9 1.0
O1 A:FMT492 2.8 23.3 1.0
C4D A:HEM491 3.0 12.4 1.0
C1D A:HEM491 3.0 12.9 1.0
C4B A:HEM491 3.0 12.8 1.0
C1B A:HEM491 3.0 12.1 1.0
C4A A:HEM491 3.0 12.0 1.0
C1A A:HEM491 3.0 11.9 1.0
CZ A:TYR337 3.1 14.4 1.0
C4C A:HEM491 3.1 12.3 1.0
C1C A:HEM491 3.1 12.1 1.0
CHB A:HEM491 3.4 11.8 1.0
CHA A:HEM491 3.4 12.2 1.0
CHD A:HEM491 3.4 11.7 1.0
CHC A:HEM491 3.4 11.4 1.0
C A:FMT492 3.8 18.9 1.0
CE1 A:TYR337 3.9 13.6 1.0
CE2 A:TYR337 3.9 14.4 1.0
NH2 A:ARG333 4.0 14.2 1.0
NE A:ARG333 4.2 15.0 1.0
C3D A:HEM491 4.2 11.6 1.0
O2 A:FMT492 4.2 18.5 1.0
C2D A:HEM491 4.2 12.3 1.0
C3B A:HEM491 4.2 11.9 1.0
C2B A:HEM491 4.3 11.4 1.0
C3A A:HEM491 4.3 13.8 1.0
C2A A:HEM491 4.3 12.5 1.0
C3C A:HEM491 4.3 12.2 1.0
CZ A:PHE140 4.3 8.2 1.0
C2C A:HEM491 4.3 12.7 1.0
CZ A:ARG333 4.5 15.4 1.0
CD2 A:HIS54 4.7 14.9 1.0
NE2 A:HIS54 4.7 13.8 1.0
CE1 A:PHE140 4.8 8.6 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: Sat Aug 3 11:41:30 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy