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Iron in PDB 1nml: Di-Haemic Cytochrome C Peroxidase From Pseudomonas Nautica 617, Form in (pH 4.0)

Enzymatic activity of Di-Haemic Cytochrome C Peroxidase From Pseudomonas Nautica 617, Form in (pH 4.0)

All present enzymatic activity of Di-Haemic Cytochrome C Peroxidase From Pseudomonas Nautica 617, Form in (pH 4.0):
1.11.1.5;

Protein crystallography data

The structure of Di-Haemic Cytochrome C Peroxidase From Pseudomonas Nautica 617, Form in (pH 4.0), PDB code: 1nml was solved by J.M.Dias, C.Bonifacio, T.Alves, A.S.Pereira, D.Bourgeois, I.Moura, M.J.Romao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.20
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 114.457, 114.457, 90.658, 90.00, 90.00, 120.00
R / Rfree (%) 17.9 / 19.9

Iron Binding Sites:

The binding sites of Iron atom in the Di-Haemic Cytochrome C Peroxidase From Pseudomonas Nautica 617, Form in (pH 4.0) (pdb code 1nml). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Di-Haemic Cytochrome C Peroxidase From Pseudomonas Nautica 617, Form in (pH 4.0), PDB code: 1nml:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1nml

Go back to Iron Binding Sites List in 1nml
Iron binding site 1 out of 2 in the Di-Haemic Cytochrome C Peroxidase From Pseudomonas Nautica 617, Form in (pH 4.0)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Di-Haemic Cytochrome C Peroxidase From Pseudomonas Nautica 617, Form in (pH 4.0) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:32.9
occ:1.00
FE A:HEM401 0.0 32.9 1.0
ND A:HEM401 2.0 31.8 1.0
NC A:HEM401 2.0 31.0 1.0
NB A:HEM401 2.0 29.8 1.0
NA A:HEM401 2.0 30.8 1.0
NE2 A:HIS55 2.1 32.9 1.0
NE2 A:HIS71 2.2 35.4 1.0
C1A A:HEM401 3.0 31.3 1.0
C1C A:HEM401 3.0 29.8 1.0
C4D A:HEM401 3.0 32.3 1.0
C1D A:HEM401 3.0 33.1 1.0
CD2 A:HIS55 3.0 32.1 1.0
C4C A:HEM401 3.0 30.5 1.0
C4B A:HEM401 3.0 29.5 1.0
C4A A:HEM401 3.1 29.5 1.0
C1B A:HEM401 3.1 28.6 1.0
CE1 A:HIS55 3.1 33.6 1.0
CE1 A:HIS71 3.2 36.1 1.0
CD2 A:HIS71 3.2 37.7 1.0
CHA A:HEM401 3.3 31.8 1.0
CHD A:HEM401 3.4 29.7 1.0
CHC A:HEM401 3.4 30.6 1.0
CHB A:HEM401 3.4 28.6 1.0
ND1 A:HIS55 4.2 34.1 1.0
CG A:HIS55 4.2 35.8 1.0
C2A A:HEM401 4.2 31.3 1.0
C2C A:HEM401 4.3 31.6 1.0
C3D A:HEM401 4.3 31.3 1.0
C3C A:HEM401 4.3 30.8 1.0
C2D A:HEM401 4.3 31.6 1.0
C3A A:HEM401 4.3 29.2 1.0
C3B A:HEM401 4.3 27.6 1.0
ND1 A:HIS71 4.3 37.4 1.0
C2B A:HEM401 4.3 27.8 1.0
CG A:HIS71 4.4 40.3 1.0

Iron binding site 2 out of 2 in 1nml

Go back to Iron Binding Sites List in 1nml
Iron binding site 2 out of 2 in the Di-Haemic Cytochrome C Peroxidase From Pseudomonas Nautica 617, Form in (pH 4.0)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Di-Haemic Cytochrome C Peroxidase From Pseudomonas Nautica 617, Form in (pH 4.0) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe402

b:34.5
occ:1.00
FE A:HEM402 0.0 34.5 1.0
ND A:HEM402 2.0 36.0 1.0
NC A:HEM402 2.0 37.6 1.0
NB A:HEM402 2.0 37.0 1.0
NA A:HEM402 2.0 36.0 1.0
NE2 A:HIS201 2.0 33.3 1.0
SD A:MET275 2.3 38.9 1.0
CE1 A:HIS201 2.9 32.9 1.0
C4D A:HEM402 3.0 36.4 1.0
C1D A:HEM402 3.0 36.1 1.0
C1C A:HEM402 3.1 36.3 1.0
C4C A:HEM402 3.1 36.4 1.0
C1A A:HEM402 3.1 35.4 1.0
C1B A:HEM402 3.1 37.4 1.0
C4A A:HEM402 3.1 36.5 1.0
C4B A:HEM402 3.1 38.2 1.0
CD2 A:HIS201 3.1 34.9 1.0
CHD A:HEM402 3.3 34.7 1.0
CHA A:HEM402 3.4 36.5 1.0
CHC A:HEM402 3.4 36.9 1.0
CHB A:HEM402 3.4 35.9 1.0
CG A:MET275 3.4 39.4 1.0
CE A:MET275 3.4 38.1 1.0
ND1 A:HIS201 4.1 34.2 1.0
CB A:MET275 4.1 38.7 1.0
CG A:HIS201 4.2 33.7 1.0
C3D A:HEM402 4.3 34.4 1.0
C2D A:HEM402 4.3 35.1 1.0
C2A A:HEM402 4.3 35.8 1.0
C3C A:HEM402 4.3 36.8 1.0
C3A A:HEM402 4.3 37.5 1.0
C2C A:HEM402 4.3 36.3 1.0
C2B A:HEM402 4.3 38.7 1.0
C3B A:HEM402 4.3 39.0 1.0

Reference:

J.M.Dias, T.Alves, A.S.Pereira, D.Bourgeois, I.Moura. Structural Basis For the Mechanism of Ca(2+) Activation of the Di-Heme Cytochrome C Peroxidase From Pseudomonas Nautica 617 Structure V. 12 961 2004.
ISSN: ISSN 0969-2126
PubMed: 15274917
DOI: 10.1016/J.STR.2004.03.025
Page generated: Sat Aug 3 11:57:17 2024

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