Structure of PDB 1qqj Chain A Binding Site BS02

Receptor Information
>1qqj 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 IDACT
InChIInChI=1S/C2H4O2/c1-2(3)4/h1H3,(H,3,4)/p-1
InChIKeyQTBSBXVTEAMEQO-UHFFFAOYSA-M
SMILES
SoftwareSMILES
ACDLabs 10.04[O-]C(=O)C
OpenEye OEToolkits 1.5.0CC(=O)[O-]
CACTVS 3.341CC([O-])=O
FormulaC2 H3 O2
NameACETATE ION
ChEMBL
DrugBankDB14511
ZINC
PDB chain1qqj Chain A Residue 2001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1qqj Crystal structure and mechanism of a carbon-carbon bond hydrolase.
Resolution1.55 Å
Binding residue
(original residue number in PDB)		Y128 V137 R142
Binding residue
(residue number reindexed from 1)		Y128 V137 R142
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D126 H133 E199 E201 D233 R237 Q240 K253 T257 E364
Catalytic site (residue number reindexed from 1) D126 H133 E199 E201 D233 R237 Q240 K253 T257 E364
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:1qqj, PDBe:1qqj, PDBj:1qqj
PDBsum1qqj
PubMed10508789
UniProtP35505|FAAA_MOUSE Fumarylacetoacetase (Gene Name=Fah)

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