Structure of PDB 1hyo Chain B Binding Site BS02
Receptor Information
>1hyo Chain B (length=419) Species:
10090
(Mus musculus) [
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GSMSFIPVAEDSDFPIQNLPYGVFSTQSNPKPRIGVAIGDQILDLSVIKH
LFTGPALSKHQHVFDETTLNNFMGLGQAAWKEARASLQNLLSASQARLRD
DKELRQRAFTSQASATMHLPATIGDYTDFYSSRQHATNVGIMFRGKENAL
LPNWLHLPVGYHGRASSIVVSGTPIRRPMGQMRPDNSKPPVYGACRLLDM
ELEMAFFVGPGNRFGEPIPISKAHEHIFGMVLMNDWSARDIQQWEYVPLG
PFLGKSFGTTISPWVVPMDALMPFVVPNPKQDPKPLPYLCHSQPYTFDIN
LSVSLKGEGMSQAATICRSNFKHMYWTMLQQLTHHSVNGCNLRPGDLLAS
GTISGSDPESFGSMLELSWKGTKAIDVGQGQTRTFLLDGDEVIITGHCQG
DGYRVGFGQCAGKVLPALS
Ligand information
Ligand ID
CA
InChI
InChI=1S/Ca/q+2
InChIKey
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
Formula
Ca
Name
CALCIUM ION
ChEMBL
DrugBank
DB14577
ZINC
PDB chain
1hyo Chain B Residue 1007 [
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Receptor-Ligand Complex Structure
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PDB
1hyo
Mechanistic inferences from the crystal structure of fumarylacetoacetate hydrolase with a bound phosphorus-based inhibitor.
Resolution
1.3 Å
Binding residue
(original residue number in PDB)
D626 E699 E701 D733
Binding residue
(residue number reindexed from 1)
D128 E201 E203 D235
Annotation score
1
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.
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:1hyo
,
PDBe:1hyo
,
PDBj:1hyo
PDBsum
1hyo
PubMed
11154690
UniProt
P35505
|FAAA_MOUSE Fumarylacetoacetase (Gene Name=Fah)
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