Structure of PDB 4c2p Chain A Binding Site BS05

Receptor Information
>4c2p Chain A (length=582) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DEAEASKFVEEYDRTSQVVWNEYAEANWNYNTNITTETSKILLQKNMQIA
NHTLKYGTQARKFDVNQLQNTTIKRIIKKVQDLERAALPAQELEEYNKIL
LDMETTYSVATVCHPNGSCLQLEPDLTNVMATSRKYEDLLWAWEGWRDKA
GRAILQFYPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLERLFQE
LQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNIYDL
VVPFPSAPSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWNKS
MLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQ
YFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSDEHD
INFLMKMALDKIAFIPFSYLVDQWRWRVFDGSITKENYNQEWWSLRLKYQ
GLCPPVPRTQGDFDPGAKFHIPSSVPYIKYFVSFIIQFQFHEALCQAAGH
TGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPNMSASAML
SYFKPLLDWLRTENELHGEKLGWPQYNWTPNS
Ligand information
Ligand IDX8Z
InChIInChI=1S/C9H15NO3S/c1-6(5-14)8(11)10-4-2-3-7(10)9(12)13/h6-7,14H,2-5H2,1H3,(H,12,13)/t6-,7+/m1/s1
InChIKeyFAKRSMQSSFJEIM-RQJHMYQMSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(O)C1N(C(=O)C(C)CS)CCC1
OpenEye OEToolkits 1.6.1C[C@H](CS)C(=O)N1CCC[C@H]1C(=O)O
CACTVS 3.352C[CH](CS)C(=O)N1CCC[CH]1C(O)=O
OpenEye OEToolkits 1.6.1CC(CS)C(=O)N1CCCC1C(=O)O
CACTVS 3.352C[C@H](CS)C(=O)N1CCC[C@H]1C(O)=O
FormulaC9 H15 N O3 S
NameL-CAPTOPRIL
ChEMBLCHEMBL1560
DrugBankDB01197
ZINCZINC000000057001
PDB chain4c2p Chain A Residue 709 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4c2p Molecular and Thermodynamic Mechanisms of the Chloride Dependent Human Angiotensin-I Converting Enzyme (Ace)
Resolution1.99 Å
Binding residue
(original residue number in PDB)		Q281 H353 A354 E384 K511 H513 Y520 Y523
Binding residue
(residue number reindexed from 1)		Q242 H314 A315 E345 K468 H470 Y477 Y480
Annotation score2
Binding affinityBindingDB: IC50=23nM,EC50=18540nM,Ki=2.0nM
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.
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:4c2p, PDBe:4c2p, PDBj:4c2p
PDBsum4c2p
PubMed24297181
UniProtP12821|ACE_HUMAN Angiotensin-converting enzyme (Gene Name=ACE)

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