Structure of PDB 1qco Chain B

Receptor sequence

>1qcoB (length=418) Species: 10090 (Mus musculus)

GSMSFIPVAEDSDFPIQNLPYGVFSTQSNPKPRIGVAIGDQILDLSVIKH
LFTGPALSKHQHVFDETTLNNFMGLGQAAWKEARASLQNLLSASQARLRD
DKELRQRAFTSQASATMHLPATIGDYTDFYSSRQHATNVGIMFRGKENAL
LPNWLHLPVGYHGRASSIVVSGTPIRRPMGQMRPDNSKPPVYGACRLLDM
ELEMAFFVGPGNRFGEPIPISKAHEHIFGMVLMNDWSARDIQQWEYVPLG
PFLGKSFGTTISPWVVPMDALMPFVVPNPKQDPKPLPYLCHSQPYTFDIN
LSVSLKGEGMSQAATICRSNFKHMYWTMLQQLTHHSVNGCNLRPGDLLAS
GTISGSDPESFGSMLELSWKGTKAIDVGQGQTRTFLLDGDEVIITGHCQG
DGYRVGFGQCAGKVLPAL

3D structure

• PDB: 1qco Crystal structure and mechanism of a carbon-carbon bond hydrolase.
• Chain: B
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D626 H633 E699 E701 D733 R737 Q740 K753 T757 E864
• Catalytic site (residue number reindexed from 1): D128 H135 E201 E203 D235 R239 Q242 K255 T259 E366
• 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	B	D626 E699 E701 D733	D128 E201 E203 D235
BS02	FUM	B	Y628 V637 R642 Q740	Y130 V139 R144 Q242
BS03	AAE	B	D626 F627 Y628 H633 Y659 E699 K753 G849 T850	D128 F129 Y130 H135 Y161 E201 K255 G351 T352

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