Structure of PDB 1qco Chain A Binding Site BS03

Receptor Information
>1qco Chain A (length=416) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MSFIPVAEDSDFPIQNLPYGVFSTQSNPKPRIGVAIGDQILDLSVIKHLF
TGPALSKHQHVFDETTLNNFMGLGQAAWKEARASLQNLLSASQARLRDDK
ELRQRAFTSQASATMHLPATIGDYTDFYSSRQHATNVGIMFRGKENALLP
NWLHLPVGYHGRASSIVVSGTPIRRPMGQMRPDNSKPPVYGACRLLDMEL
EMAFFVGPGNRFGEPIPISKAHEHIFGMVLMNDWSARDIQQWEYVPLGPF
LGKSFGTTISPWVVPMDALMPFVVPNPKQDPKPLPYLCHSQPYTFDINLS
VSLKGEGMSQAATICRSNFKHMYWTMLQQLTHHSVNGCNLRPGDLLASGT
ISGSDPESFGSMLELSWKGTKAIDVGQGQTRTFLLDGDEVIITGHCQGDG
YRVGFGQCAGKVLPAL
Ligand information
Ligand IDAAE
InChIInChI=1S/C4H6O3/c1-3(5)2-4(6)7/h2H2,1H3,(H,6,7)
InChIKeyWDJHALXBUFZDSR-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(=O)CC(=O)O
ACDLabs 10.04O=C(C)CC(=O)O
CACTVS 3.341CC(=O)CC(O)=O
FormulaC4 H6 O3
NameACETOACETIC ACID
ChEMBLCHEMBL1230762
DrugBankDB01762
ZINCZINC000000895089
PDB chain1qco Chain A Residue 1010 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1qco Crystal structure and mechanism of a carbon-carbon bond hydrolase.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		D126 F127 Y128 H133 Y159 E199 K253 G349 T350
Binding residue
(residue number reindexed from 1)		D126 F127 Y128 H133 Y159 E199 K253 G349 T350
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K253
Catalytic site (residue number reindexed from 1) K253
Enzyme Commision number 3.7.1.2: fumarylacetoacetase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004334 fumarylacetoacetase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0006527 arginine catabolic process
GO:0006559 L-phenylalanine catabolic process
GO:0006572 tyrosine catabolic process
GO:0006629 lipid metabolic process
GO:0009072 aromatic amino acid metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1qco, PDBe:1qco, PDBj:1qco
PDBsum1qco
PubMed10508789
UniProtP35505|FAAA_MOUSE Fumarylacetoacetase (Gene Name=Fah)

[Back to BioLiP]