Structure of PDB 2hzy Chain A Binding Site BS01

Receptor Information
>2hzy Chain A (length=416) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MSFIPVAEDSDFPIQNLPYGVFSTQSNPKPRIGVAIGDQILDLSVIKHLF
TGPALSKHQHVFDETTLNNFMGLGQAAWKEARASLQNLLSASQARLRDDK
ELRQRAFTSQASATMHLPATIGDYTDFYSSRQHATNVGIMFRGKENALLP
NWLHLPVGYHGRASSIVVSGTPIRRPMGQMRPDNSKPPVYGACRLLDMEL
EMAFFVGPGNRFGEPIPISKAHEHIFGMVLMNDWSARDIQQWEYVPLGPF
LGKSFGTTISPWVVPMDALMPFVVPNPKQDPKPLPYLCHSQPYTFDINLS
VSLKGEGMSQAATICRSNFKHMYWTMLQQLTHHSVNGCNLRPGDLLASGT
ISGSDPESFGSMLELSWKGTKAIDVGQGQTRTFLLDGDEVIITGHCQGDG
YRVGFGQCAGKVLPAL
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain2hzy Chain A Residue 1203 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2hzy Slow-onset inhibition of fumarylacetoacetate hydrolase by phosphinate mimics of the tetrahedral intermediate: kinetics, crystal structure and pharmacokinetics.
Resolution1.35 Å
Binding residue
(original residue number in PDB)		D126 E199 E201 D233
Binding residue
(residue number reindexed from 1)		D126 E199 E201 D233
Annotation score1
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.
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

View graph for
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)

[Back to BioLiP]