Structure of PDB 3hok Chain A

Receptor sequence
>3hokA (length=214) Species: 9606 (Homo sapiens) [Search protein sequence]
PQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYV
ALEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTP
AMQRYVKRLHEVGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPS
SGEGLAFFTFPNIASATKFKQLYRSRMNSLEMTPAVRQRVIEEAKTAFLL
NIQLFEELQELLTH
3D structure
PDB3hok X-ray crystal structure of human heme oxygenase-1 with (2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4[((5-trifluoromethylpyridin-2-yl)thio)methyl]-1,3-dioxolane: a novel, inducible binding mode.
ChainA
Resolution2.19 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) N30 Y58 T135 R136 G139 D140 G144
Catalytic site (residue number reindexed from 1) N21 Y49 T126 R127 G130 D131 G135
Enzyme Commision number 1.14.14.18: heme oxygenase (biliverdin-producing).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 HEM A H25 A28 E29 M34 Y134 T135 G139 F207 N210 F214 H16 A19 E20 M25 Y125 T126 G130 F198 N201 F205
Gene Ontology
Molecular Function
GO:0004392 heme oxygenase (decyclizing) activity
Biological Process
GO:0006788 heme oxidation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3hok, PDBe:3hok, PDBj:3hok
PDBsum3hok
PubMed19601578
UniProtP09601|HMOX1_HUMAN Heme oxygenase 1 (Gene Name=HMOX1)

[Back to BioLiP]