Structure of PDB 4aa2 Chain A Binding Site BS01

Receptor Information

>4aa2 Chain A (length=598) Species: 7227 (Drosophila melanogaster)

ALVKEEIQAKEYLENLNKELAKRTNVETEAAWAYGSNITDENEKKKNEIS
AELAKFMKEVASDTTKFQWRSYQSEDLKRQFKALTKLGYAALPEDDYAEL
LDTLSAMESNFAKVKVCDYKDSTKCDLALDPEIEEVISKSRDHEELAYYW
REFYDKAGTAVRSQFERYVELNTKAAKLNNFTSGAEAWLDEYEDDTFEQQ
LEDIFADIRPLYQQIHGYVRFRLRKHYGDAVVSETGPIPMHLLGNMWAQQ
WSEIADIVSPFPEKPLVDVSAEMEKQGYTPLKMFQMGDDFFTSMNLTKLP
QDFWDKSIIEKPTDGRDLVCHASAWDFYLTDDVRIKQCTRVTQDQLFTVH
HELGHIQYFLQYQHQPFVYRTGANPGFHEAVGDVLSLSVSTPKHLEKIGL
LKDYVRDDEARINQLFLTALDKIVFLPFAFTMDKYRWSLFRGEVDKANWN
CAFWKLRDEYSGIEPPVVRSEKDFDAPAKYHISADVEYLRYLVSFIIQFQ
FYKSACIKAGQYDPDNVELPLDNCDIYGSAAAGAAFHNMLSMGASKPWPD
ALEAFNGERIMSGKAIAEYFEPLRVWLEAENIKNNVHIGWTTSNKCVS

Ligand information

>4aa2 Chain P (length=6) Species: 242054 (Gloydius blomhoffii)

RPKIPP

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4aa2 Structural Basis of Peptide Recognition by the Angiotensin-I Converting Enzyme Homologue Ance from Drosophila Melanogaster
• Resolution: 1.99 Å
• Binding residue (original residue number in PDB): Q265 H337 A338 S339 A340 W341 H367 E368 H371 H394 F441 K495 Y496 H497 D501 Y504 Y507
• Binding residue (residue number reindexed from 1): Q249 H321 A322 S323 A324 W325 H351 E352 H355 H378 F425 K479 Y480 H481 D485 Y488 Y491

Enzymatic activity

• Catalytic site (original residue number in PDB): H337 A338 H367 E368 H371 E395 H497 Y507
• Catalytic site (residue number reindexed from 1): H321 A322 H351 E352 H355 E379 H481 Y491
• Enzyme Commision number: 3.4.15.1: peptidyl-dipeptidase A.

Gene Ontology

Molecular Function

• GO:0008237 metallopeptidase activity
• GO:0008241 peptidyl-dipeptidase activity

Biological Process

• GO:0006508 proteolysis

Cellular Component

• GO:0016020 membrane

External links

• PDB: RCSB:4aa2, PDBe:4aa2, PDBj:4aa2
• PDBsum: 4aa2
• PubMed: 23082758
• UniProt: Q10714|ACE_DROME Angiotensin-converting enzyme (Gene Name=Ance)