Atomistry » Iron » PDB 2c2c-2ciy » 2cah
Atomistry »
  Iron »
    PDB 2c2c-2ciy »
      2cah »

Iron in PDB 2cah: Structure of Proteus Mirabilis Pr Catalase For the Native Form (E- Fe(III)) Complexed with Nadph

Enzymatic activity of Structure of Proteus Mirabilis Pr Catalase For the Native Form (E- Fe(III)) Complexed with Nadph

All present enzymatic activity of Structure of Proteus Mirabilis Pr Catalase For the Native Form (E- Fe(III)) Complexed with Nadph:
1.11.1.6;

Protein crystallography data

The structure of Structure of Proteus Mirabilis Pr Catalase For the Native Form (E- Fe(III)) Complexed with Nadph, PDB code: 2cah was solved by P.Gouet, H.-M.Jouve, O.Dideberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.70
Space group P 62 2 2
Cell size a, b, c (Å), α, β, γ (°) 112.360, 112.360, 249.140, 90.00, 90.00, 120.00
R / Rfree (%) 19.6 / n/a

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Proteus Mirabilis Pr Catalase For the Native Form (E- Fe(III)) Complexed with Nadph (pdb code 2cah). 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 Structure of Proteus Mirabilis Pr Catalase For the Native Form (E- Fe(III)) Complexed with Nadph, PDB code: 2cah:

Iron binding site 1 out of 1 in 2cah

Go back to Iron Binding Sites List in 2cah
Iron binding site 1 out of 1 in the Structure of Proteus Mirabilis Pr Catalase For the Native Form (E- Fe(III)) Complexed with Nadph


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Proteus Mirabilis Pr Catalase For the Native Form (E- Fe(III)) Complexed with Nadph within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe485

b:15.3
occ:1.00
 FE A:HEM485 0.0 15.3 1.0
OH A:TYR337 1.8 16.1 1.0
ND A:HEM485 1.9 15.2 1.0
NB A:HEM485 1.9 8.9 1.0
NC A:HEM485 1.9 17.6 1.0
NA A:HEM485 2.0 13.4 1.0
CZ A:TYR337 2.8 15.5 1.0
C4D A:HEM485 3.0 15.4 1.0
C1B A:HEM485 3.0 15.6 1.0
C4B A:HEM485 3.0 10.7 1.0
C1D A:HEM485 3.0 19.1 1.0
C1C A:HEM485 3.0 17.2 1.0
C4C A:HEM485 3.0 22.3 1.0
C1A A:HEM485 3.0 13.1 1.0
C4A A:HEM485 3.0 13.1 1.0
O A:HOH490 3.3 30.1 1.0
CHA A:HEM485 3.3 9.2 1.0
CHC A:HEM485 3.4 9.6 1.0
CHD A:HEM485 3.4 20.0 1.0
CHB A:HEM485 3.4 14.9 1.0
CE1 A:TYR337 3.6 16.5 1.0
CE2 A:TYR337 3.6 15.4 1.0
C3D A:HEM485 4.2 12.9 1.0
C3B A:HEM485 4.2 10.8 1.0
NE A:ARG333 4.2 8.4 1.0
C2D A:HEM485 4.2 15.0 1.0
C2B A:HEM485 4.2 8.9 1.0
C2C A:HEM485 4.2 17.8 1.0
C3C A:HEM485 4.2 18.1 1.0
C2A A:HEM485 4.2 9.3 1.0
C3A A:HEM485 4.2 12.8 1.0
NH2 A:ARG333 4.3 11.8 1.0
CZ A:PHE140 4.4 12.9 1.0
CZ A:ARG333 4.7 13.4 1.0
CD1 A:TYR337 4.8 11.2 1.0
NE2 A:HIS54 4.8 16.0 1.0
CD2 A:HIS54 4.9 16.1 1.0
CD2 A:TYR337 4.9 8.1 1.0
CE2 A:PHE140 4.9 13.8 1.0

Reference:

P.Gouet, H.M.Jouve, O.Dideberg. Crystal Structure of Proteus Mirabilis Pr Catalase with and Without Bound Nadph. J.Mol.Biol. V. 249 933 1995.
ISSN: ISSN 0022-2836
PubMed: 7791219
DOI: 10.1006/JMBI.1995.0350
Page generated: Sat Aug 3 20:09:10 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy