Structure of PDB 1lc0 Chain A

Receptor sequence
>1lc0A (length=290) Species: 10116 (Rattus norvegicus) [Search protein sequence]
MITNSGKFGVVVVGVGRAGSVRLRDLKDPRSAAFLNLIGFVSRRELGSLD
EVRQISLEDALRSQEIDVAYICSESSSHEDYIRQFLQAGKHVLVEYPMTL
SFAAAQELWELAAQKGRVLHEEHVELLMEEFEFLRREVLGKELLKGSLRF
TASPLEEERFGFPAFSGISRLTWLVSLFGELSLISATLEERKEDQYMKMT
VQLETQNKGLLSWIEEKGPGLKRNRYVNFQFTSGSLEEVPSVGVNKNIFL
KDQDIFVQKLLDQVSAEDLAAEKKRIMHCLGLASDIQKLC
3D structure
PDB1lc0 Crystal structure of a biliverdin IXalpha reductase enzyme-cofactor complex.
ChainA
Resolution1.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E96 Y97 E123 E126 S170 R171
Catalytic site (residue number reindexed from 1) E95 Y96 E122 E125 S169 R170
Enzyme Commision number 1.3.1.24: biliverdin reductase.
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 PO4 A V16 S43 R44 R45 V15 S42 R43 R44
BS02 PO4 A S102 F103 A104 S285 S101 F102 A103 S284
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0004074 biliverdin reductase [NAD(P)+] activity
GO:0008270 zinc ion binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0106276 biliberdin reductase (NAD+) activity
GO:0106277 biliverdin reductase (NADP+) activity
Biological Process
GO:0042167 heme catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1lc0, PDBe:1lc0, PDBj:1lc0
PDBsum1lc0
PubMed12079357
UniProtP46844|BIEA_RAT Biliverdin reductase A (Gene Name=Blvra)

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