Structure of PDB 4mec Chain A

Receptor sequence
>4mecA (length=214) Species: 10116 (Rattus norvegicus) [Search protein sequence]
SQDLSEALKEATKEVHIRAENSEFMRNFQKGQVSREGFKLVMASLYHIYT
ALEEEIERNKQNPVYAPLYFPEELHRRAALEQDMAFWYGPHWQEAIPYTP
ATQHYVKRLHEVGGTHPELLVAHAYTRYLGDLSGGQVLKKIAQKAMALPS
SGEGLAFFTFPSIDNPTKFKQLYRARMNTLEMTPEVKHRVTEEAKTAFLL
NIELFEELQALLTE
3D structure
PDB4mec Distal regulation of heme binding of heme oxygenase-1 mediated by conformational fluctuations
ChainA
Resolution3.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 ZNH A K18 H25 E29 Q38 Y134 T135 G139 S142 G143 L147 R183 F207 K9 H16 E20 Q29 Y125 T126 G130 S133 G134 L138 R174 F198
Gene Ontology
Molecular Function
GO:0004392 heme oxygenase (decyclizing) activity
Biological Process
GO:0006788 heme oxidation

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Molecular Function

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Biological Process
External links
PDB RCSB:4mec, PDBe:4mec, PDBj:4mec
PDBsum4mec
PubMed25496210
UniProtP06762|HMOX1_RAT Heme oxygenase 1 (Gene Name=Hmox1)

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