Structure of PDB 2hzy Chain B

Receptor sequence
>2hzyB (length=418) Species: 10090 (Mus musculus) [Search protein sequence]
GSMSFIPVAEDSDFPIQNLPYGVFSTQSNPKPRIGVAIGDQILDLSVIKH
LFTGPALSKHQHVFDETTLNNFMGLGQAAWKEARASLQNLLSASQARLRD
DKELRQRAFTSQASATMHLPATIGDYTDFYSSRQHATNVGIMFRGKENAL
LPNWLHLPVGYHGRASSIVVSGTPIRRPMGQMRPDNSKPPVYGACRLLDM
ELEMAFFVGPGNRFGEPIPISKAHEHIFGMVLMNDWSARDIQQWEYVPLG
PFLGKSFGTTISPWVVPMDALMPFVVPNPKQDPKPLPYLCHSQPYTFDIN
LSVSLKGEGMSQAATICRSNFKHMYWTMLQQLTHHSVNGCNLRPGDLLAS
GTISGSDPESFGSMLELSWKGTKAIDVGQGQTRTFLLDGDEVIITGHCQG
DGYRVGFGQCAGKVLPAL
3D structure
PDB2hzy Slow-onset inhibition of fumarylacetoacetate hydrolase by phosphinate mimics of the tetrahedral intermediate: kinetics, crystal structure and pharmacokinetics.
ChainB
Resolution1.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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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) 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 G122 D123 G124 D125
BS02 MN B D126 E199 E201 D233 D128 E201 E203 D235
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

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2hzy, PDBe:2hzy, PDBj:2hzy
PDBsum2hzy
PubMed17064256
UniProtP35505|FAAA_MOUSE Fumarylacetoacetase (Gene Name=Fah)

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