Structure of PDB 4pv4 Chain B

Receptor sequence

>4pv4B (length=436) Species: 632 (Yersinia pestis)

MTQQEYQNRRQALLAKMAPGSAAIIFAAPEATRSADSEYPYRQNSDFSYL
TGFNEPEAVLILVKSDETHNHSVLFNRIRDLTAEIWFGRRLGQEAAPTKL
AVDRALPFDEINEQLYLLLNRLDVIYHAQGQYAYADNIVFAALEKLRHGF
RKNLRAPATLTDWRPWLHEMRLFKSAEEIAVLRRAGEISALAHTRAMEKC
RPGMFEYQLEGEILHEFTRHGARYPAYNTIVGGGENGCILHYTENECELR
DGDLVLIDAGCEYRGYAGDITRTFPVNGKFTPAQRAVYDIVLAAINKSLT
LFRPGTSIREVTEEVVRIMVVGLVELGILKGDIEQLIAEQAHRPFFMHGL
SHWLGMDVHDVGDYGSSDRGRILEPGMVLTVEPGLYIAPDADVPPQYRGI
GIRIEDDIVITATGNENLTASVVKDPDDIEALMALN

3D structure

• PDB: 4pv4 Proline aminopeptidase P II from Yersinia pestis
• Chain: B
• Resolution: 1.76 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D36 H241 D258 D269 H348 H352 H359 E382 Y386 R403 E405
• Catalytic site (residue number reindexed from 1): D36 H241 D258 D269 H348 H352 H359 E382 Y386 R403 E405
• 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	MG	B	D269 H352 E382 E405	D269 H352 E382 E405
BS02	MG	B	D258 D269 E405	D258 D269 E405

Gene Ontology

Molecular Function

• GO:0004177 aminopeptidase activity
• GO:0008235 metalloexopeptidase activity
• GO:0008237 metallopeptidase activity
• GO:0030145 manganese ion binding
• GO:0046872 metal ion binding
• GO:0046914 transition metal ion binding
• GO:0070006 metalloaminopeptidase activity

Biological Process

• GO:0006508 proteolysis

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:4pv4, PDBe:4pv4, PDBj:4pv4
• PDBsum: 4pv4
• UniProt: A0A2S9PFE9