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Iron in PDB 4pwv: Structure of P450SKY (CYP163B3), A Cytochrome P450 From Skyllamycin Biosynthesis in Complex with A Peptidyl Carrier Protein Domain

Enzymatic activity of Structure of P450SKY (CYP163B3), A Cytochrome P450 From Skyllamycin Biosynthesis in Complex with A Peptidyl Carrier Protein Domain

All present enzymatic activity of Structure of P450SKY (CYP163B3), A Cytochrome P450 From Skyllamycin Biosynthesis in Complex with A Peptidyl Carrier Protein Domain:
1.14.14.1;

Protein crystallography data

The structure of Structure of P450SKY (CYP163B3), A Cytochrome P450 From Skyllamycin Biosynthesis in Complex with A Peptidyl Carrier Protein Domain, PDB code: 4pwv was solved by K.Haslinger, M.J.Cryle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.62 / 3.00
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 95.260, 95.260, 336.800, 90.00, 90.00, 120.00
R / Rfree (%) 23.3 / 27.7

Iron Binding Sites:

The binding sites of Iron atom in the Structure of P450SKY (CYP163B3), A Cytochrome P450 From Skyllamycin Biosynthesis in Complex with A Peptidyl Carrier Protein Domain (pdb code 4pwv). 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 P450SKY (CYP163B3), A Cytochrome P450 From Skyllamycin Biosynthesis in Complex with A Peptidyl Carrier Protein Domain, PDB code: 4pwv:

Iron binding site 1 out of 1 in 4pwv

Go back to Iron Binding Sites List in 4pwv
Iron binding site 1 out of 1 in the Structure of P450SKY (CYP163B3), A Cytochrome P450 From Skyllamycin Biosynthesis in Complex with A Peptidyl Carrier Protein Domain


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of P450SKY (CYP163B3), A Cytochrome P450 From Skyllamycin Biosynthesis in Complex with A Peptidyl Carrier Protein Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:42.6
occ:1.00
FE A:HEM501 0.0 42.6 1.0
N3 B:KH4101 2.0 47.5 1.0
NA A:HEM501 2.0 42.6 1.0
NC A:HEM501 2.1 42.9 1.0
NB A:HEM501 2.1 43.0 1.0
ND A:HEM501 2.1 42.4 1.0
SG A:CYS357 2.3 45.1 1.0
C4 B:KH4101 2.6 48.9 1.0
C4A A:HEM501 3.0 42.5 1.0
C1A A:HEM501 3.0 42.6 1.0
C4C A:HEM501 3.1 42.9 1.0
C1B A:HEM501 3.1 43.0 1.0
C1C A:HEM501 3.1 42.9 1.0
C4B A:HEM501 3.1 43.1 1.0
C1D A:HEM501 3.1 42.4 1.0
C4D A:HEM501 3.1 42.3 1.0
C2 B:KH4101 3.2 49.3 1.0
CHB A:HEM501 3.4 42.5 1.0
CB A:CYS357 3.4 45.8 1.0
CHA A:HEM501 3.4 42.6 1.0
CHD A:HEM501 3.4 42.5 1.0
CHC A:HEM501 3.4 43.0 1.0
C5 B:KH4101 4.0 51.5 1.0
CA A:CYS357 4.1 45.9 1.0
N4 B:KH4101 4.2 49.6 1.0
C2A A:HEM501 4.3 42.5 1.0
C3A A:HEM501 4.3 42.6 1.0
C3C A:HEM501 4.3 43.6 1.0
C2B A:HEM501 4.3 42.9 1.0
C2C A:HEM501 4.3 43.4 1.0
C3B A:HEM501 4.3 43.0 1.0
C2D A:HEM501 4.3 42.0 1.0
C3D A:HEM501 4.3 41.9 1.0
N A:LEU358 4.6 46.5 1.0
N A:GLY359 4.7 47.6 1.0
C A:CYS357 4.7 46.2 1.0

Reference:

K.Haslinger, C.Brieke, S.Uhlmann, L.Sieverling, R.D.Sussmuth, M.J.Cryle. The Structure of A Transient Complex of A Nonribosomal Peptide Synthetase and A Cytochrome P450 Monooxygenase. Angew.Chem.Int.Ed.Engl. V. 53 8518 2014.
ISSN: ISSN 1433-7851
PubMed: 25044735
DOI: 10.1002/ANIE.201404977
Page generated: Mon Aug 5 08:31:51 2024

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