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Chlorine in PDB 1n3u: Crystal Structure of Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B

Enzymatic activity of Crystal Structure of Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B

All present enzymatic activity of Crystal Structure of Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B:
1.14.99.3;

Protein crystallography data

The structure of Crystal Structure of Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B, PDB code: 1n3u was solved by L.Lad, D.J.Schuller, J.P.Friedman, H.Li, P.R.Ortiz Demontellano, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 70.00 / 2.58
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 54.395, 55.920, 79.379, 90.00, 101.20, 90.00
R / Rfree (%) 22.5 / 26.5

Other elements in 1n3u:

The structure of Crystal Structure of Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B (pdb code 1n3u). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B, PDB code: 1n3u:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 1n3u

Go back to Chlorine Binding Sites List in 1n3u
Chlorine binding site 1 out of 3 in the Crystal Structure of Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl234

b:62.3
occ:1.00
OG1 A:THR176 3.4 56.2 1.0
N A:ALA175 3.8 50.2 1.0
N A:THR176 3.9 52.2 1.0
CB A:ALA175 4.1 49.9 1.0
OG A:SER174 4.3 53.2 1.0
CB A:THR176 4.4 54.6 1.0
CA A:ALA175 4.4 50.9 1.0
C A:SER174 4.6 50.8 1.0
CA A:SER174 4.6 50.8 1.0
C A:ALA175 4.7 51.5 1.0
CA A:THR176 4.8 53.1 1.0
CB A:SER174 5.0 52.0 1.0

Chlorine binding site 2 out of 3 in 1n3u

Go back to Chlorine Binding Sites List in 1n3u
Chlorine binding site 2 out of 3 in the Crystal Structure of Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl234

b:67.4
occ:1.00
CE B:LYS153 4.3 82.9 1.0

Chlorine binding site 3 out of 3 in 1n3u

Go back to Chlorine Binding Sites List in 1n3u
Chlorine binding site 3 out of 3 in the Crystal Structure of Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Human Heme Oxygenase 1 (Ho-1) in Complex with Its Substrate Heme, Crystal Form B within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl235

b:75.1
occ:1.00
OG B:SER174 3.4 51.5 1.0
OG1 B:THR176 3.7 52.8 1.0
N B:ALA175 3.8 48.3 1.0
CA B:SER174 3.8 49.0 1.0
CB B:SER174 4.0 49.8 1.0
N B:THR176 4.1 50.7 1.0
C B:SER174 4.2 48.4 1.0
CB B:THR176 4.3 51.8 1.0
CA B:ALA175 4.7 49.1 1.0
CB B:ALA175 4.8 48.5 1.0
O B:ALA173 4.8 48.1 1.0
CA B:THR176 4.8 51.0 1.0
C B:ALA175 4.9 50.1 1.0

Reference:

L.Lad, D.J.Schuller, H.Shimizu, J.Friedman, H.Li, P.R.Ortiz De Montellano, T.L.Poulos. Comparison of the Heme-Free and -Bound Crystal Structures of Human Heme Oxygenase-1 J.Biol.Chem. V. 278 7834 2003.
ISSN: ISSN 0021-9258
PubMed: 12500973
DOI: 10.1074/JBC.M211450200
Page generated: Thu Jul 10 18:18:26 2025

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