Structure of PDB 1ft7 Chain A Binding Site BS02
Receptor Information
>1ft7 Chain A (length=291) Species:
671
(Vibrio proteolyticus) [
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MPPITQQATVTAWLPQVDASQITGTISSLESFTNRFYTTTSGAQASDWIA
SEWQALSASLPNASVKQVSHSGYNQKSVVMTITGSEAPDEWIVIGGHLDS
TIGSHTNEQSVAPGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAA
EEVGLRGSQDLANQYKSEGKNVVSALQLDMTNYKGSAQDVVFITDYTDSN
FTQYLTQLMDEYLPSLTYGFDTCGYACSDHASWHNAGYPAAMPFESKFND
YNPRIHTTQDTLANSDPTGSHAKKFTQLGLAYAIEMGSATG
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
1ft7 Chain A Residue 502 [
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Receptor-Ligand Complex Structure
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PDB
1ft7
Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinephosphonic acid. Spectroscopic and crystallographic characterization of the transition state of peptide hydrolysis.
Resolution
2.2 Å
Binding residue
(original residue number in PDB)
H97 D117 D179
Binding residue
(residue number reindexed from 1)
H97 D117 D179
Annotation score
4
Enzymatic activity
Catalytic site (original residue number in PDB)
H97 D117 E151 E152 D179 H256
Catalytic site (residue number reindexed from 1)
H97 D117 E151 E152 D179 H256
Enzyme Commision number
3.4.11.10
: bacterial leucyl aminopeptidase.
Gene Ontology
Molecular Function
GO:0008235
metalloexopeptidase activity
Biological Process
GO:0006508
proteolysis
View graph for
Molecular Function
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Biological Process
External links
PDB
RCSB:1ft7
,
PDBe:1ft7
,
PDBj:1ft7
PDBsum
1ft7
PubMed
11401547
UniProt
Q01693
|AMPX_VIBPR Bacterial leucyl aminopeptidase
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