Structure of PDB 2v3y Chain A Binding Site BS01

Receptor Information

>2v3y Chain A (length=440) Species: 562 (Escherichia coli)

SEISRQEFQRRRQALVEQMQPGSAALIFAAPEVTRSADSEYPYRQNSDFW
YFTGFNEPEAVLVLIKSDDTHNHSVLFNRVRDLTAEIWFGRRLGQDAAPE
KLGVDRALAFSEINQQLYQLLNGLDVVYHAQGEYAYADVIVNSALEKLRK
GSRQNLTAPATMIDWRPVVHEMRLFKSPEEIAVLRRAGEITAMAHTRAME
KCRPGMFEYHLEGEIHHEFNRHGARYPSYNTIVGSGENGCILHYTENECE
MRDGDLVLIDAGCEYKGYAGDITRTFPVNGKFTQAQREIYDIVLESLETS
LRLYRPGTSILEVTGEVVRIMVSGLVKLGILKGDVDELIAQNAHRPFFMH
GLSHWLGLDVADVGVYGQDRSRILEPGMVLTVEPGLYIAPDAEVPEQYRG
IGIRIEDDIVITETGNENLTASVVKKPEEIEALMVAARKQ

Ligand information

>2v3y Chain B (length=2) Species: 562 (Escherichia coli)

PL

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2v3y Complexes of Mutants of Escherichia Coli Aminopeptidase P and the Tripeptide Substrate Valproleu.
• Resolution: 1.6 Å
• Binding residue (original residue number in PDB): H243 H350 G351 E383 R404
• Binding residue (residue number reindexed from 1): H243 H350 G351 E383 R404

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

External links

• PDB: RCSB:2v3y, PDBe:2v3y, PDBj:2v3y
• PDBsum: 2v3y
• PubMed: 17983589
• UniProt: P15034|AMPP_ECOLI Xaa-Pro aminopeptidase (Gene Name=pepP)