Structure of PDB 1qcn Chain B

Receptor sequence

>1qcnB (length=419) Species: 10090 (Mus musculus)

GSMSFIPVAEDSDFPIQNLPYGVFSTQSNPKPRIGVAIGDQILDLSVIKH
LFTGPALSKHQHVFDETTLNNFMGLGQAAWKEARASLQNLLSASQARLRD
DKELRQRAFTSQASATMHLPATIGDYTDFYSSRQHATNVGIMFRGKENAL
LPNWLHLPVGYHGRASSIVVSGTPIRRPMGQMRPDNSKPPVYGACRLLDM
ELEMAFFVGPGNRFGEPIPISKAHEHIFGMVLMNDWSARDIQQWEYVPLG
PFLGKSFGTTISPWVVPMDALMPFVVPNPKQDPKPLPYLCHSQPYTFDIN
LSVSLKGEGMSQAATICRSNFKHMYWTMLQQLTHHSVNGCNLRPGDLLAS
GTISGSDPESFGSMLELSWKGTKAIDVGQGQTRTFLLDGDEVIITGHCQG
DGYRVGFGQCAGKVLPALS

3D structure

• PDB: 1qcn 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	L916 S917	L418 S419
BS02	CA	B	D626 E699 E701 D733 K753	D128 E201 E203 D235 K255
BS03	ACT	B	Y659 K753	Y161 K255
BS04	ACT	B	Y628 R642	Y130 R144

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