Structure of PDB 1qqj Chain A

Receptor sequence

>1qqjA (length=416) Species: 10090 (Mus musculus)

MSFIPVAEDSDFPIQNLPYGVFSTQSNPKPRIGVAIGDQILDLSVIKHLF
TGPALSKHQHVFDETTLNNFMGLGQAAWKEARASLQNLLSASQARLRDDK
ELRQRAFTSQASATMHLPATIGDYTDFYSSRQHATNVGIMFRGKENALLP
NWLHLPVGYHGRASSIVVSGTPIRRPMGQMRPDNSKPPVYGACRLLDMEL
EMAFFVGPGNRFGEPIPISKAHEHIFGMVLMNDWSARDIQQWEYVPLGPF
LGKSFGTTISPWVVPMDALMPFVVPNPKQDPKPLPYLCHSQPYTFDINLS
VSLKGEGMSQAATICRSNFKHMYWTMLQQLTHHSVNGCNLRPGDLLASGT
ISGSDPESFGSMLELSWKGTKAIDVGQGQTRTFLLDGDEVIITGHCQGDG
YRVGFGQCAGKVLPAL

3D structure

• PDB: 1qqj Crystal structure and mechanism of a carbon-carbon bond hydrolase.
• Chain: A
• Resolution: 1.55 Å

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.

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	CA	A	D126 E199 E201 D233	D126 E199 E201 D233
BS02	ACT	A	Y128 V137 R142	Y128 V137 R142

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

External links

• PDB: RCSB:1qqj, PDBe:1qqj, PDBj:1qqj
• PDBsum: 1qqj
• PubMed: 10508789
• UniProt: P35505|FAAA_MOUSE Fumarylacetoacetase (Gene Name=Fah)