Structure of PDB 1w2m Chain C Binding Site BS01

Receptor Information
>1w2m Chain C (length=439) 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
GLSHWLGLDVHDVGVYGQDRSRILEPGMVLTVEPGLYIAPDAEVPEQYRG
IGIRIEDDIVITETGNENLTASVVKKPEEIEALMVAARK
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain1w2m Chain C Residue 1441 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1w2m Structural and Functional Implications of Metal Ion Selection in Aminopeptidase P, a Metalloprotease with a Dinuclear Metal Center.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		D271 H354 E383 E406
Binding residue
(residue number reindexed from 1)		D271 H354 E383 E406
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D38 H243 D260 D271 H350 H354 H361 E383 Y387 R404 E406
Catalytic site (residue number reindexed from 1) D38 H243 D260 D271 H350 H354 H361 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:1w2m, PDBe:1w2m, PDBj:1w2m
PDBsum1w2m
PubMed16229471
UniProtP15034|AMPP_ECOLI Xaa-Pro aminopeptidase (Gene Name=pepP)

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