Structure of PDB 1hyo Chain A Binding Site BS01
Receptor Information
>1hyo 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 ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
1hyo Chain A Residue 1004 [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
Receptor-Ligand Complex Structure
Global view
Local view
Structure 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
]
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)
D233 W234 K253 G256 T257
Binding residue
(residue number reindexed from 1)
D233 W234 K253 G256 T257
Annotation score
1
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:1hyo
,
PDBe:1hyo
,
PDBj:1hyo
PDBsum
1hyo
PubMed
11154690
UniProt
P35505
|FAAA_MOUSE Fumarylacetoacetase (Gene Name=Fah)
[
Back to BioLiP
]