Structure of PDB 1lc3 Chain A Binding Site BS03
Receptor Information
>1lc3 Chain A (length=292) Species:
10116
(Rattus norvegicus) [
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MITNSGKFGVVVVGVGRAGSVRLRDLKDPRSAAFLNLIGFVSRRELGSLD
EVRQISLEDALRSQEIDVAYICSESSSHEDYIRQFLQAGKHVLVEYPMTL
SFAAAQELWELAAQKGRVLHEEHVELLMEEFEFLRREVLGKELLKGSLRF
TASPLEEERFGFPAFSGISRLTWLVSLFGELSLISATLEERKEDQYMKMT
VQLETQNKGLLSWIEEKGPGLKRNRYVNFQFTSGSLEEVPSVGVNKNIFL
KDQDIFVQKLLDQVSAEDLAAEKKRIMHCLGLASDIQKLCHQ
Ligand information
Ligand ID
PO4
InChI
InChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKey
NBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
Software
SMILES
CACTVS 3.341
[O-][P]([O-])([O-])=O
ACDLabs 10.04
[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0
[O-]P(=O)([O-])[O-]
Formula
O4 P
Name
PHOSPHATE ION
ChEMBL
DrugBank
DB14523
ZINC
PDB chain
1lc3 Chain A Residue 604 [
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Receptor-Ligand Complex Structure
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PDB
1lc3
Crystal structure of a biliverdin IXalpha reductase enzyme-cofactor complex.
Resolution
1.5 Å
Binding residue
(original residue number in PDB)
F151 R171 R224
Binding residue
(residue number reindexed from 1)
F150 R170 R223
Annotation score
1
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.
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:1lc3
,
PDBe:1lc3
,
PDBj:1lc3
PDBsum
1lc3
PubMed
12079357
UniProt
P46844
|BIEA_RAT Biliverdin reductase A (Gene Name=Blvra)
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