Structure of PDB 1vix Chain B

Receptor sequence
>1vixB (length=410) Species: 562 (Escherichia coli) [Search protein sequence]
MSLDKLLERFLNYVSLDTQSKAGVRQVPSTEGQWKLLHLLKEQLEEMGLI
NVTLSEKGTLMATLPANVPGDIPAIGFISHVDTSPDCSGKNVNPQIVENY
RGGDIALGIGDEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGIAEI
MTALAVLQQKKIPHGDIRVAFTPDEEVGKGAKHFDVDAFDARWAYTVDGG
GVGELEFENFNAASVNIKIVGNNVHPGTAKGVMVNALSLAARIHAEVPAD
ESPEMTEGYEGFYHLASMKGTVERADMHYIIRDFDRKQFEARKRKMMEIA
KKVGKGLHPDCYIELVIEDSYYNMREKVVEHPHILDIAQQAMRDCDIEPE
LKPIRGGTDGAQLSFMGLPCPNLFTGGYNYHGKHEFVTLEGMEKAVQVIV
RIAELTAQRK
3D structure
PDB1vix Structural analysis of a set of proteins resulting from a bacterial genomics project
ChainB
Resolution2.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.11.4: tripeptide aminopeptidase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN B H78 D140 D196 H80 D142 D198
BS02 ZN B D140 E174 H379 D142 E176 H381
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

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Cellular Component
External links
PDB RCSB:1vix, PDBe:1vix, PDBj:1vix
PDBsum1vix
PubMed16021622
UniProtP29745|PEPT_ECOLI Peptidase T (Gene Name=pepT)

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