Structure of PDB 2prq Chain A Binding Site BS01
Receptor Information
>2prq Chain A (length=291) Species:
671
(Vibrio proteolyticus) [
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MPPITQQATVTAWLPQVDASQITGTISSLESFTNRFYTTTSGAQASDWIA
SEWQALSASLPNASVKQVSHSGYNQKSVVMTITGSEAPDEWIVIGGHLDS
TIGSHTNEQSVAPGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAA
EEVGLRGSQDLANQYKSEGKNVVSALQLDMTNYKGSAQDVVFITDYTDSN
FTQYLTQLMDEYLPSLTYGFDTCGYACSDHASWHNAGYPAAMPFESKFND
YNPRIHTTQDTLANSDPTGSHAKKFTQLGLAYAIEMGSATG
Ligand information
Ligand ID
CO
InChI
InChI=1S/Co/q+2
InChIKey
XLJKHNWPARRRJB-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Co+2]
CACTVS 3.341
[Co++]
Formula
Co
Name
COBALT (II) ION
ChEMBL
DrugBank
DB14205
ZINC
PDB chain
2prq Chain A Residue 501 [
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Receptor-Ligand Complex Structure
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PDB
2prq
X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica.
Resolution
2.15 Å
Binding residue
(original residue number in PDB)
D117 E152 H256
Binding residue
(residue number reindexed from 1)
D117 E152 H256
Annotation score
3
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
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Molecular Function
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Biological Process
External links
PDB
RCSB:2prq
,
PDBe:2prq
,
PDBj:2prq
PDBsum
2prq
PubMed
17574677
UniProt
Q01693
|AMPX_VIBPR Bacterial leucyl aminopeptidase
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