Structure of PDB 2bwt Chain A

Receptor sequence

>2bwtA (length=440) Species: 562 (Escherichia coli)

SEISRQEFQRRRQALVEQMQPGSAALIFAAPEVTRSADSEYPYRQNSDFW
YFTGFNEPEAVLVLIKSDDTHNHSVLFNRVRDLTAEIWFGRRLGQDAAPE
KLGVDRALAFSEINQQLYQLLNGLDVVYHAQGEYAYADVIVNSALEKLRK
GSRQNLTAPATMIDWRPVVHEMRLFKSPEEIAVLRRAGEITAMAHTRAME
KCRPGMFEYHLEGEIHHEFNRHGARYPSYNTIVGSGENGCILHYTENECE
MRDGDLVLIAAGCEYKGYAGDITRTFPVNGKFTQAQREIYDIVLESLETS
LRLYRPGTSILEVTGEVVRIMVSGLVKLGILKGDVDELIAQNAHRPFFMH
GLSHWLGLDVHDVGVYGQDRSRILEPGMVLTVEPGLYIAPDAEVPEQYRG
IGIRIEDDIVITETGNENLTASVVKKPEEIEALMVAARKQ

3D structure

• PDB: 2bwt Kinetic and Crystallographic Analysis of Mutant Escherichia Coli Aminopeptidase P: Insights Into Substrate Recognition and the Mechanism of Catalysis.
• Chain: A
• Resolution: 2.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D38 H243 A260 D271 H350 H354 H361 E383 Y387 R404 E406
• Catalytic site (residue number reindexed from 1): D38 H243 A260 D271 H350 H354 H361 E383 Y387 R404 E406
• Enzyme Commision number: 3.4.11.9: Xaa-Pro 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	MN	A	D271 H354 T381 E383 E406	D271 H354 T381 E383 E406

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:2bwt, PDBe:2bwt, PDBj:2bwt
• PDBsum: 2bwt
• PubMed: 16411772
• UniProt: P15034|AMPP_ECOLI Xaa-Pro aminopeptidase (Gene Name=pepP)