Structure of PDB 2x96 Chain A

Receptor sequence
>2x96A (length=598) Species: 7227 (Drosophila melanogaster) [Search protein sequence]
ALVKEEIQAKEYLENLNKELAKRTNVETEAAWAYGSNITDENEKKKNEIS
AELAKFMKEVASDTTKFQWRSYQSEDLKRQFKALTKLGYAALPEDDYAEL
LDTLSAMESNFAKVKVCDYKDSTKCDLALDPEIEEVISKSRDHEELAYYW
REFYDKAGTAVRSQFERYVELNTKAAKLNNFTSGAEAWLDEYEDDTFEQQ
LEDIFADIRPLYQQIHGYVRFRLRKHYGDAVVSETGPIPMHLLGNMWAQQ
WSEIADIVSPFPEKPLVDVSAEMEKQGYTPLKMFQMGDDFFTSMNLTKLP
QDFWDKSIIEKPTDGRDLVCHASAWDFYLTDDVRIKQCTRVTQDQLFTVH
HELGHIQYFLQYQHQPFVYRTGANPGFHEAVGDVLSLSVSTPKHLEKIGL
LKDYVRDDEARINQLFLTALDKIVFLPFAFTMDKYRWSLFRGEVDKANWN
CAFWKLRDEYSGIEPPVVRSEKDFDAPAKYHISADVEYLRYLVSFIIQFQ
FYKSACIKAGQYDPDNVELPLDNCDIYGSAAAGAAFHNMLSMGASKPWPD
ALEAFNGERIMSGKAIAEYFEPLRVWLEAENIKNNVHIGWTTSNKCVS
3D structure
PDB2x96 High Resolution Crystal Structures of Drosophila Melanogaster Angiotensin Converting Enzyme in Complex with Novel Inhibitors and Anti- Hypertensive Drugs.
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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.
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 RX3 A Q266 H337 A338 S339 A340 H367 E368 H371 F375 H394 E395 D399 F441 K495 H497 V502 Y504 Y507 Q250 H321 A322 S323 A324 H351 E352 H355 F359 H378 E379 D383 F425 K479 H481 V486 Y488 Y491 MOAD: Ki=94uM
PDBbind-CN: -logKd/Ki=4.03,Ki=94uM
BS02 ZN A H367 H371 E395 H351 H355 E379
Gene Ontology
Molecular Function
GO:0008237 metallopeptidase activity
GO:0008241 peptidyl-dipeptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0016020 membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2x96, PDBe:2x96, PDBj:2x96
PDBsum2x96
PubMed20488190
UniProtQ10714|ACE_DROME Angiotensin-converting enzyme (Gene Name=Ance)

[Back to BioLiP]