Structure of PDB 1twr Chain A

Receptor sequence
>1twrA (length=214) Species: 9606 (Homo sapiens) [Search protein sequence]
PQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYV
ALEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTP
AMQRYVKRLHEVGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPS
SGEGLAFFTFPNIASATKFKQLYRSRMNSLEMTPAVRQRVIEEAKTAFLL
NIQLFEELQELLTH
3D structure
PDB1twr Crystal structures of ferrous and ferrous-NO forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage.
ChainA
Resolution2.1 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 VER A K18 H25 Q38 Y134 T135 G139 S142 F207 N210 F214 K9 H16 Q29 Y125 T126 G130 S133 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:1twr, PDBe:1twr, PDBj:1twr
PDBsum1twr
PubMed15522396
UniProtP09601|HMOX1_HUMAN Heme oxygenase 1 (Gene Name=HMOX1)

[Back to BioLiP]