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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: Thu Jul 17 00:21:54 2025

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