Structure of PDB 2hzy Chain A

Receptor sequence

>2hzyA (length=416) Species: 10090 (Mus musculus)

MSFIPVAEDSDFPIQNLPYGVFSTQSNPKPRIGVAIGDQILDLSVIKHLF
TGPALSKHQHVFDETTLNNFMGLGQAAWKEARASLQNLLSASQARLRDDK
ELRQRAFTSQASATMHLPATIGDYTDFYSSRQHATNVGIMFRGKENALLP
NWLHLPVGYHGRASSIVVSGTPIRRPMGQMRPDNSKPPVYGACRLLDMEL
EMAFFVGPGNRFGEPIPISKAHEHIFGMVLMNDWSARDIQQWEYVPLGPF
LGKSFGTTISPWVVPMDALMPFVVPNPKQDPKPLPYLCHSQPYTFDINLS
VSLKGEGMSQAATICRSNFKHMYWTMLQQLTHHSVNGCNLRPGDLLASGT
ISGSDPESFGSMLELSWKGTKAIDVGQGQTRTFLLDGDEVIITGHCQGDG
YRVGFGQCAGKVLPAL

3D structure

• PDB: 2hzy Slow-onset inhibition of fumarylacetoacetate hydrolase by phosphinate mimics of the tetrahedral intermediate: kinetics, crystal structure and pharmacokinetics.
• Chain: A
• Resolution: 1.35 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	MN	A	D126 E199 E201 D233	D126 E199 E201 D233
BS02	CA	A	G122 D123	G122 D123

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:2hzy, PDBe:2hzy, PDBj:2hzy
• PDBsum: 2hzy
• PubMed: 17064256
• UniProt: P35505|FAAA_MOUSE Fumarylacetoacetase (Gene Name=Fah)