Structure of PDB 1qcn Chain B Binding Site BS03
Receptor Information
>1qcn 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
ACT
InChI
InChI=1S/C2H4O2/c1-2(3)4/h1H3,(H,3,4)/p-1
InChIKey
QTBSBXVTEAMEQO-UHFFFAOYSA-M
SMILES
Software
SMILES
ACDLabs 10.04
[O-]C(=O)C
OpenEye OEToolkits 1.5.0
CC(=O)[O-]
CACTVS 3.341
CC([O-])=O
Formula
C2 H3 O2
Name
ACETATE ION
ChEMBL
DrugBank
DB14511
ZINC
PDB chain
1qcn Chain B Residue 1006 [
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Receptor-Ligand Complex Structure
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PDB
1qcn
Crystal structure and mechanism of a carbon-carbon bond hydrolase.
Resolution
1.9 Å
Binding residue
(original residue number in PDB)
Y659 K753
Binding residue
(residue number reindexed from 1)
Y161 K255
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:1qcn
,
PDBe:1qcn
,
PDBj:1qcn
PDBsum
1qcn
PubMed
10508789
UniProt
P35505
|FAAA_MOUSE Fumarylacetoacetase (Gene Name=Fah)
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