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Iron in PDB 1bva: Manganese Binding Mutant in Cytochrome C Peroxidase

Enzymatic activity of Manganese Binding Mutant in Cytochrome C Peroxidase

All present enzymatic activity of Manganese Binding Mutant in Cytochrome C Peroxidase:
1.11.1.5;

Protein crystallography data

The structure of Manganese Binding Mutant in Cytochrome C Peroxidase, PDB code: 1bva was solved by S.K.Wilcox, D.E.Mcree, D.B.Goodin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.89
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 105.800, 73.600, 50.500, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / n/a

Other elements in 1bva:

The structure of Manganese Binding Mutant in Cytochrome C Peroxidase also contains other interesting chemical elements:

Manganese (Mn) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Manganese Binding Mutant in Cytochrome C Peroxidase (pdb code 1bva). 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 Manganese Binding Mutant in Cytochrome C Peroxidase, PDB code: 1bva:

Iron binding site 1 out of 1 in 1bva

Go back to Iron Binding Sites List in 1bva
Iron binding site 1 out of 1 in the Manganese Binding Mutant in Cytochrome C Peroxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Manganese Binding Mutant in Cytochrome C Peroxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe390

b:10.2
occ:1.00
FE A:HEM390 0.0 10.2 1.0
NA A:HEM390 2.0 6.7 1.0
NE2 A:HIS175 2.0 7.6 1.0
NB A:HEM390 2.1 3.8 1.0
NC A:HEM390 2.1 12.4 1.0
ND A:HEM390 2.1 2.9 1.0
O A:HOH776 2.3 15.0 1.0
CE1 A:HIS175 3.0 9.3 1.0
C1A A:HEM390 3.0 9.2 1.0
C4A A:HEM390 3.0 5.9 1.0
C4B A:HEM390 3.0 2.1 1.0
CD2 A:HIS175 3.0 10.2 1.0
C1B A:HEM390 3.0 6.0 1.0
C1C A:HEM390 3.1 9.7 1.0
C4D A:HEM390 3.1 6.0 1.0
C1D A:HEM390 3.1 10.8 1.0
C4C A:HEM390 3.1 16.6 1.0
CHB A:HEM390 3.3 7.4 1.0
CHC A:HEM390 3.4 2.6 1.0
CHA A:HEM390 3.4 12.3 1.0
CHD A:HEM390 3.4 6.5 1.0
NE1 A:TRP51 4.0 9.5 1.0
ND1 A:HIS175 4.1 7.7 1.0
CG A:HIS175 4.2 9.6 1.0
C2A A:HEM390 4.2 14.8 1.0
C3A A:HEM390 4.2 7.9 1.0
C3D A:HEM390 4.2 8.8 1.0
O A:HOH656 4.2 14.0 1.0
C3B A:HEM390 4.2 7.4 1.0
C2B A:HEM390 4.3 9.8 1.0
C2C A:HEM390 4.3 11.7 1.0
C3C A:HEM390 4.3 14.1 1.0
C2D A:HEM390 4.3 10.6 1.0
O A:HOH481 4.3 24.3 1.0
CD1 A:TRP51 4.6 5.3 1.0
CH2 A:TRP191 4.9 6.5 1.0

Reference:

S.K.Wilcox, C.D.Putnam, M.Sastry, J.Blankenship, W.J.Chazin, D.E.Mcree, D.B.Goodin. Rational Design of A Functional Metalloenzyme: Introduction of A Site For Manganese Binding and Oxidation Into A Heme Peroxidase. Biochemistry V. 37 16853 1998.
ISSN: ISSN 0006-2960
PubMed: 9836578
DOI: 10.1021/BI9815039
Page generated: Sun Dec 13 14:08:12 2020

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