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Bromine in PDB 1ged: A Positive Charge Route For the Access of Nadh to Heme Formed in the Distal Heme Pocket of Cytochrome P450NOR

Protein crystallography data

The structure of A Positive Charge Route For the Access of Nadh to Heme Formed in the Distal Heme Pocket of Cytochrome P450NOR, PDB code: 1ged was solved by T.Kudo, N.Takaya, S.-Y.Park, Y.Shiro, H.Shoun, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 54.320, 78.050, 86.600, 90.00, 90.00, 90.00
R / Rfree (%) 21.4 / 27.9

Other elements in 1ged:

The structure of A Positive Charge Route For the Access of Nadh to Heme Formed in the Distal Heme Pocket of Cytochrome P450NOR also contains other interesting chemical elements:

Iron (Fe) 1 atom

Bromine Binding Sites:

The binding sites of Bromine atom in the A Positive Charge Route For the Access of Nadh to Heme Formed in the Distal Heme Pocket of Cytochrome P450NOR (pdb code 1ged). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the A Positive Charge Route For the Access of Nadh to Heme Formed in the Distal Heme Pocket of Cytochrome P450NOR, PDB code: 1ged:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in 1ged

Go back to Bromine Binding Sites List in 1ged
Bromine binding site 1 out of 2 in the A Positive Charge Route For the Access of Nadh to Heme Formed in the Distal Heme Pocket of Cytochrome P450NOR


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of A Positive Charge Route For the Access of Nadh to Heme Formed in the Distal Heme Pocket of Cytochrome P450NOR within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br404

b:29.4
occ:1.00
O A:THR168 2.7 20.7 1.0
OG A:SER150 2.9 21.2 1.0
ND2 A:ASN171 3.0 25.6 1.0
CB A:ASN171 3.1 23.3 1.0
C A:THR168 3.6 25.4 1.0
CG A:ASN171 3.6 25.5 1.0
ND2 A:ASN241 3.6 21.8 1.0
CD1 A:LEU146 3.6 25.1 1.0
O A:HOH562 3.6 33.7 1.0
CA A:THR168 3.7 26.5 1.0
CB A:SER150 3.7 22.3 1.0
N A:ALA172 3.9 21.1 1.0
C A:ASN171 4.0 20.4 1.0
CA A:ASN171 4.0 19.6 1.0
CG2 A:THR168 4.1 25.0 1.0
CB A:THR168 4.4 27.2 1.0
O A:LEU167 4.4 25.9 1.0
N A:ASN171 4.5 16.5 1.0
CA A:ALA172 4.6 22.8 1.0
CG A:ASN241 4.6 16.0 1.0
O A:ASN171 4.6 25.0 1.0
CE2 A:TYR154 4.6 25.4 1.0
CB A:ALA172 4.7 27.5 1.0
OG1 A:THR168 4.7 26.5 1.0
CG A:LEU146 4.7 25.8 1.0
OH A:TYR154 4.8 20.0 1.0
OD1 A:ASN171 4.8 29.6 1.0
CA A:SER150 4.8 19.1 1.0
N A:GLN169 4.8 21.6 1.0
N A:THR168 4.9 25.7 1.0

Bromine binding site 2 out of 2 in 1ged

Go back to Bromine Binding Sites List in 1ged
Bromine binding site 2 out of 2 in the A Positive Charge Route For the Access of Nadh to Heme Formed in the Distal Heme Pocket of Cytochrome P450NOR


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of A Positive Charge Route For the Access of Nadh to Heme Formed in the Distal Heme Pocket of Cytochrome P450NOR within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br405

b:30.4
occ:1.00
O A:SER286 2.6 24.0 1.0
OD1 A:ASN315 2.9 26.0 1.0
N A:ALA289 3.0 19.6 1.0
CB A:ALA289 3.3 17.8 1.0
ND2 A:ASN315 3.3 20.1 1.0
CMA A:HEM501 3.4 10.1 1.0
CG A:ASN315 3.4 27.6 1.0
C A:SER286 3.4 18.6 1.0
CA A:ALA289 3.5 20.1 1.0
C A:ALA287 3.5 21.3 1.0
CA A:ALA287 3.6 18.9 1.0
N A:LEU288 3.6 22.4 1.0
N A:ILE290 3.8 21.9 1.0
O A:HOH522 3.8 26.1 1.0
CG1 A:ILE290 3.8 24.3 1.0
N A:ALA287 3.8 18.7 1.0
C A:ALA289 4.0 21.4 1.0
O A:ALA287 4.1 22.1 1.0
C A:LEU288 4.1 21.6 1.0
OG A:SER286 4.1 22.1 1.0
O A:HOH541 4.3 28.6 1.0
CA A:LEU288 4.4 21.9 1.0
CB A:SER286 4.5 19.2 1.0
CA A:SER286 4.5 19.4 1.0
C3A A:HEM501 4.6 16.4 1.0
CB A:ASN315 4.7 27.1 1.0
CB A:ILE290 4.8 21.0 1.0
CAA A:HEM501 4.8 16.0 1.0
CD1 A:ILE290 4.8 28.9 1.0
CA A:ILE290 4.8 22.9 1.0

Reference:

T.Kudo, N.Takaya, S.-Y.Park, Y.Shiro, H.Shoun. A Positively Charged Cluster Formed in the Heme-Distal Pocket of Cytochrome P450NOR Is Essential For Interaction with Nadh J.Biol.Chem. V. 276 5020 2001.
ISSN: ISSN 0021-9258
PubMed: 11076941
DOI: 10.1074/JBC.M007244200
Page generated: Mon Jul 7 03:12:53 2025

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