Structure of PDB 2xy9 Chain A

Receptor sequence
>2xy9A (length=581) Species: 9606 (Homo sapiens) [Search protein sequence]
DEAEASKFVEEYDRTSQVVWNEYAEANWNYNTNITTETSKILLQKNMQIA
NHTLKYGTQARKFDVNQLQNTTIKRIIKKVQDLERAALPAQELEEYNKIL
LDMETTYSVATVCHPNGSCLQLEPDLTNVMATSRKYEDLLWAWEGWRDKA
GRAILQFYPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLERLFQE
LQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNIYDL
VVPFPSAPSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWNKS
MLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQ
YFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSDEHD
INFLMKMALDKIAFIPFSYLVDQWRWRVFDGSITKENYNQEWWSLRLKYQ
GLCPPVPRTQGDFDPGAKFHIPSSVPYIRYFVSFIIQFQFHEALCQAAGH
TGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPNMSASAML
SYFKPLLDWLRTENELHGEKLGWPQYNWTPA
3D structure
PDB2xy9 Novel Mechanism of Inhibition of Human Angiotensin-I-Converting Enzyme (Ace) by a Highly Specific Phosphinic Tripeptide.
ChainA
Resolution1.97 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H353 A354 H383 E384 H387 E411 H513 Y523
Catalytic site (residue number reindexed from 1) H314 A315 H344 E345 H348 E372 H470 Y480
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 FUC A S45 E49 S6 E10
BS02 ZN A H383 H387 E411 H344 H348 E372
BS03 3ES A Q281 H353 A354 S355 A356 E376 V380 H383 E384 H387 F391 H410 F457 K511 F512 H513 V518 Y520 Y523 F527 Q242 H314 A315 S316 A317 E337 V341 H344 E345 H348 F352 H371 F414 K468 F469 H470 V475 Y477 Y480 F484 MOAD: Ki=0.65nM
PDBbind-CN: -logKd/Ki=9.19,Ki=0.65nM
BindingDB: Ki=0.65nM
BS04 3ES A W59 Y62 N66 E123 W220 M223 W357 P519 R522 W20 Y23 N27 E84 W181 M184 W318 P476 R479 MOAD: Ki=0.65nM
PDBbind-CN: -logKd/Ki=9.19,Ki=0.65nM
BindingDB: Ki=0.65nM
Gene Ontology
Molecular Function
GO:0008237 metallopeptidase activity
GO:0008241 peptidyl-dipeptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0016020 membrane

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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2xy9, PDBe:2xy9, PDBj:2xy9
PDBsum2xy9
PubMed21352096
UniProtP12821|ACE_HUMAN Angiotensin-converting enzyme (Gene Name=ACE)

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