Structure of PDB 1qco Chain A Binding Site BS01
Receptor Information
>1qco Chain A (length=416) Species:
10090
(Mus musculus) [
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MSFIPVAEDSDFPIQNLPYGVFSTQSNPKPRIGVAIGDQILDLSVIKHLF
TGPALSKHQHVFDETTLNNFMGLGQAAWKEARASLQNLLSASQARLRDDK
ELRQRAFTSQASATMHLPATIGDYTDFYSSRQHATNVGIMFRGKENALLP
NWLHLPVGYHGRASSIVVSGTPIRRPMGQMRPDNSKPPVYGACRLLDMEL
EMAFFVGPGNRFGEPIPISKAHEHIFGMVLMNDWSARDIQQWEYVPLGPF
LGKSFGTTISPWVVPMDALMPFVVPNPKQDPKPLPYLCHSQPYTFDINLS
VSLKGEGMSQAATICRSNFKHMYWTMLQQLTHHSVNGCNLRPGDLLASGT
ISGSDPESFGSMLELSWKGTKAIDVGQGQTRTFLLDGDEVIITGHCQGDG
YRVGFGQCAGKVLPAL
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
1qco Chain A Residue 1002 [
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Receptor-Ligand Complex Structure
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PDB
1qco
Crystal structure and mechanism of a carbon-carbon bond hydrolase.
Resolution
1.9 Å
Binding residue
(original residue number in PDB)
D126 E199 E201 D233
Binding residue
(residue number reindexed from 1)
D126 E199 E201 D233
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
K253
Catalytic site (residue number reindexed from 1)
K253
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:1qco
,
PDBe:1qco
,
PDBj:1qco
PDBsum
1qco
PubMed
10508789
UniProt
P35505
|FAAA_MOUSE Fumarylacetoacetase (Gene Name=Fah)
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