Structure of PDB 1vix Chain B Binding Site BS01
Receptor Information
>1vix Chain B (length=410) Species:
562
(Escherichia coli) [
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MSLDKLLERFLNYVSLDTQSKAGVRQVPSTEGQWKLLHLLKEQLEEMGLI
NVTLSEKGTLMATLPANVPGDIPAIGFISHVDTSPDCSGKNVNPQIVENY
RGGDIALGIGDEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGIAEI
MTALAVLQQKKIPHGDIRVAFTPDEEVGKGAKHFDVDAFDARWAYTVDGG
GVGELEFENFNAASVNIKIVGNNVHPGTAKGVMVNALSLAARIHAEVPAD
ESPEMTEGYEGFYHLASMKGTVERADMHYIIRDFDRKQFEARKRKMMEIA
KKVGKGLHPDCYIELVIEDSYYNMREKVVEHPHILDIAQQAMRDCDIEPE
LKPIRGGTDGAQLSFMGLPCPNLFTGGYNYHGKHEFVTLEGMEKAVQVIV
RIAELTAQRK
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
1vix Chain B Residue 419 [
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Receptor-Ligand Complex Structure
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PDB
1vix
Structural analysis of a set of proteins resulting from a bacterial genomics project
Resolution
2.5 Å
Binding residue
(original residue number in PDB)
H78 D140 D196
Binding residue
(residue number reindexed from 1)
H80 D142 D198
Annotation score
4
Enzymatic activity
Enzyme Commision number
3.4.11.4
: tripeptide aminopeptidase.
Gene Ontology
Molecular Function
GO:0004177
aminopeptidase activity
GO:0005515
protein binding
GO:0008237
metallopeptidase activity
GO:0008270
zinc ion binding
GO:0016787
hydrolase activity
GO:0042803
protein homodimerization activity
GO:0045148
tripeptide aminopeptidase activity
GO:0046872
metal ion binding
Biological Process
GO:0006508
proteolysis
GO:0006518
peptide metabolic process
GO:0043171
peptide catabolic process
Cellular Component
GO:0005737
cytoplasm
GO:0005829
cytosol
View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1vix
,
PDBe:1vix
,
PDBj:1vix
PDBsum
1vix
PubMed
16021622
UniProt
P29745
|PEPT_ECOLI Peptidase T (Gene Name=pepT)
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