Structure of PDB 2ydm Chain A

Receptor sequence
>2ydmA (length=574) Species: 9606 (Homo sapiens) [Search protein sequence]
DEAEASKFVEEYDRTSQVVWNEYAEANWNYNTNITTETSKILLQKNMQIA
NHTLKYGTQARKFDVNQLQNTTIKRIIKKVQDLERAALPAQELEEYNKIL
LDMETTYSVATVCHPNGSCLQLEPDLTNVMATSRKYEDLLWAWEGWRDKA
GRAILQFYPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLERLFQE
LQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNIYDL
VVPFPSAPSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWNKS
MLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQ
YFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSDEHD
INFLMKMALDKIAFIPFSYLVDQWRWRVFDGSITKENYNQEWWSLRLKYQ
GLCPPVPRTQGDFDPGAKFHIPSSVPYIRYFVSFIIQFQFHEALCQAAGH
TGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPNMSASAML
SYFKPLLDWLRTENELHGEKLGWQ
3D structure
PDB2ydm Structural Characterization of Angiotensin-I Converting Enzyme in Complex with a Selenium Analogue of Captopril
ChainA
Resolution2.44 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 ZN A H383 H387 E411 H344 H348 E372
BS02 SLC A Q281 H353 H383 E384 K511 H513 Y520 Y523 Q242 H314 H344 E345 K468 H470 Y477 Y480 MOAD: ic50=36.4nM
PDBbind-CN: -logKd/Ki=7.44,IC50=36.4nM
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

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Cellular Component
External links
PDB RCSB:2ydm, PDBe:2ydm, PDBj:2ydm
PDBsum2ydm
PubMed21810173
UniProtP12821|ACE_HUMAN Angiotensin-converting enzyme (Gene Name=ACE)

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