Structure of PDB 1w7v Chain D Binding Site BS03
Receptor Information
>1w7v Chain D (length=439) Species:
562
(Escherichia coli) [
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SEISRQEFQRRRQALVEQMQPGSAALIFAAPEVTRSADSEYPYRQNSDFW
YFTGFNEPEAVLVLIKSDDTHNHSVLFNRVRDLTAEIWFGRRLGQDAAPE
KLGVDRALAFSEINQQLYQLLNGLDVVYHAQGEYAYADVIVNSALEKLRK
GSRQNLTAPATMIDWRPVVHEMRLFKSPEEIAVLRRAGEITAMAHTRAME
KCRPGMFEYHLEGEIHHEFNRHGARYPSYNTIVGSGENGCILHYTENECE
MRDGDLVLIDAGCEYKGYAGDITRTFPVNGKFTQAQREIYDIVLESLETS
LRLYRPGTSILEVTGEVVRIMVSGLVKLGILKGDVDELIAQNAHRPFFMH
GLSHWLGLDVHDVGVYGQDRSRILEPGMVLTVEPGLYIAPDAEVPEQYRG
IGIRIEDDIVITETGNENLTASVVKKPEEIEALMVAARK
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
1w7v Chain D Residue 1441 [
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Receptor-Ligand Complex Structure
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PDB
1w7v
Structural and Functional Implications of Metal Ion Selection in Aminopeptidase P, a Metalloprotease with a Dinuclear Metal Center.
Resolution
2.0 Å
Binding residue
(original residue number in PDB)
D260 D271 E406
Binding residue
(residue number reindexed from 1)
D260 D271 E406
Annotation score
4
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
View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1w7v
,
PDBe:1w7v
,
PDBj:1w7v
PDBsum
1w7v
PubMed
16229471
UniProt
P15034
|AMPP_ECOLI Xaa-Pro aminopeptidase (Gene Name=pepP)
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