Structure of PDB 1wbq Chain B

Receptor sequence

>1wbqB (length=439) Species: 562 (Escherichia coli)

SEISRQEFQRRRQALVEQMQPGSAALIFAAPEVTRSADSEYPYRQNSDFW
YFTGFNEPEAVLVLIKSDDTHNHSVLFNRVRDLTAEIWFGRRLGQDAAPE
KLGVDRALAFSEINQQLYQLLNGLDVVYHAQGEYAYADVIVNSALEKLRK
GSRQNLTAPATMIDWRPVVHEMRLFKSPEEIAVLRRAGEITAMAHTRAME
KCRPGMFEYHLEGEIHHEFNRHGARYPSYNTIVGSGENGCILHYTENECE
MRDGDLVLIDAGCEYKGYAGDITRTFPVNGKFTQAQREIYDIVLESLETS
LRLYRPGTSILEVTGEVVRIMVSGLVKLGILKGDVDELIAQNAHRPFFMH
GLSHWLGLDVHDVGVYGQDRSRILEPGMVLTVEPGLYIAPDAEVPEQYRG
IGIRIEDDIVITETGNENLTASVVKKPEEIEALMVAARK

3D structure

• PDB: 1wbq Structural and Functional Implications of Metal Ion Selection in Aminopeptidase P, a Metalloprotease with a Dinuclear Metal Center.
• Chain: B
• Resolution: 2.3 Å

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.

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	D271 H354 E383 E406	D271 H354 E383 E406
BS02	MG	B	D260 D271 E406	D260 D271 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:1wbq, PDBe:1wbq, PDBj:1wbq
• PDBsum: 1wbq
• PubMed: 16229471
• UniProt: P15034|AMPP_ECOLI Xaa-Pro aminopeptidase (Gene Name=pepP)