Structure of PDB 1amp Chain A Binding Site BS01
Receptor Information
>1amp 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
1amp Chain A Residue 501 [
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Receptor-Ligand Complex Structure
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PDB
1amp
Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family.
Resolution
1.8 Å
Binding residue
(original residue number in PDB)
D117 E152 H256
Binding residue
(residue number reindexed from 1)
D117 E152 H256
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
View graph for
Biological Process
External links
PDB
RCSB:1amp
,
PDBe:1amp
,
PDBj:1amp
PDBsum
1amp
PubMed
8087555
UniProt
Q01693
|AMPX_VIBPR Bacterial leucyl aminopeptidase
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