Structure of PDB 4asq Chain A Binding Site BS01

Receptor Information

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

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

Ligand information

>4asq Chain P (length=3) Species: 9606 (Homo sapiens)

RPP

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4asq 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 H367 E368 H371 F441 K495 H497 Y504 Y507
• Binding residue (residue number reindexed from 1): Q249 H321 A322 H351 E352 H355 F425 K479 H481 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:4asq, PDBe:4asq, PDBj:4asq
• PDBsum: 4asq
• PubMed: 23082758
• UniProt: Q10714|ACE_DROME Angiotensin-converting enzyme (Gene Name=Ance)