Calcium in PDB 3qfr: Crystal Structure of Human Nadph-Cytochrome P450 Reductase (R457H Mutant)

Enzymatic activity of Crystal Structure of Human Nadph-Cytochrome P450 Reductase (R457H Mutant)

All present enzymatic activity of Crystal Structure of Human Nadph-Cytochrome P450 Reductase (R457H Mutant):
1.6.2.4;

Protein crystallography data

The structure of Crystal Structure of Human Nadph-Cytochrome P450 Reductase (R457H Mutant), PDB code: 3qfr was solved by C.Xia, C.Marohnic, S.P.Panda, B.S.Masters, J.-J.P.Kim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.72 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 70.276, 120.393, 156.345, 90.00, 90.00, 90.00
R / Rfree (%) 22.7 / 28.5

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Human Nadph-Cytochrome P450 Reductase (R457H Mutant) (pdb code 3qfr). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Human Nadph-Cytochrome P450 Reductase (R457H Mutant), PDB code: 3qfr:

Calcium binding site 1 out of 1 in 3qfr

Go back to Calcium Binding Sites List in 3qfr
Calcium binding site 1 out of 1 in the Crystal Structure of Human Nadph-Cytochrome P450 Reductase (R457H Mutant)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Human Nadph-Cytochrome P450 Reductase (R457H Mutant) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca761

b:89.3
occ:1.00
OD1 A:ASN595 2.9 49.0 1.0
CG A:ASN595 3.6 50.4 1.0
OD1 A:ASP615 3.8 58.6 1.0
OD2 A:ASP615 4.2 57.5 1.0
ND2 A:ASN595 4.3 53.3 1.0
NE2 A:GLN593 4.3 54.7 1.0
CB A:ASN595 4.4 50.0 1.0
CG A:ASP615 4.4 57.1 1.0
CD A:GLN593 4.9 59.0 1.0

Reference:

C.Xia, S.P.Panda, C.C.Marohnic, P.Martasek, B.S.Masters, J.J.Kim. Structural Basis For Human Nadph-Cytochrome P450 Oxidoreductase Deficiency. Proc.Natl.Acad.Sci.Usa V. 108 13486 2011.
ISSN: ISSN 0027-8424
PubMed: 21808038
DOI: 10.1073/PNAS.1106632108
Page generated: Sat Dec 12 04:26:49 2020

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