Structure of PDB 2v3y Chain A Binding Site BS03

Receptor Information
>2v3y Chain A (length=440) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SEISRQEFQRRRQALVEQMQPGSAALIFAAPEVTRSADSEYPYRQNSDFW
YFTGFNEPEAVLVLIKSDDTHNHSVLFNRVRDLTAEIWFGRRLGQDAAPE
KLGVDRALAFSEINQQLYQLLNGLDVVYHAQGEYAYADVIVNSALEKLRK
GSRQNLTAPATMIDWRPVVHEMRLFKSPEEIAVLRRAGEITAMAHTRAME
KCRPGMFEYHLEGEIHHEFNRHGARYPSYNTIVGSGENGCILHYTENECE
MRDGDLVLIDAGCEYKGYAGDITRTFPVNGKFTQAQREIYDIVLESLETS
LRLYRPGTSILEVTGEVVRIMVSGLVKLGILKGDVDELIAQNAHRPFFMH
GLSHWLGLDVADVGVYGQDRSRILEPGMVLTVEPGLYIAPDAEVPEQYRG
IGIRIEDDIVITETGNENLTASVVKKPEEIEALMVAARKQ
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain2v3y Chain A Residue 1442 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2v3y Complexes of Mutants of Escherichia Coli Aminopeptidase P and the Tripeptide Substrate Valproleu.
Resolution1.6 Å
Binding residue
(original residue number in PDB)		D260 D271 E406
Binding residue
(residue number reindexed from 1)		D260 D271 E406
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D38 H243 D260 D271 H350 H354 A361 E383 Y387 R404 E406
Catalytic site (residue number reindexed from 1) D38 H243 D260 D271 H350 H354 A361 E383 Y387 R404 E406
Enzyme Commision number 3.4.11.9: Xaa-Pro aminopeptidase.
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0005515 protein binding
GO:0008235 metalloexopeptidase activity
GO:0008237 metallopeptidase activity
GO:0030145 manganese ion binding
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0046914 transition metal ion binding
GO:0070006 metalloaminopeptidase activity
Biological Process
GO:0006508 proteolysis
GO:0051289 protein homotetramerization
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0032991 protein-containing complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2v3y, PDBe:2v3y, PDBj:2v3y
PDBsum2v3y
PubMed17983589
UniProtP15034|AMPP_ECOLI Xaa-Pro aminopeptidase (Gene Name=pepP)

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