Structure of PDB 6f9v Chain A

Receptor sequence
>6f9vA (length=605) Species: 9606 (Homo sapiens) [Search protein sequence]
LDPGLQPGQFSADEAGAQLFAQSYQSSAEQVLFQSVAASWAHDTNITAEN
ARRQEEAALLSQEFAEAWGQKAKELYEPIWQQFTDPQLRRIIGAVRTLGS
ANLPLAKRQQYNALLSQMSRIYSTAKVCLATCWSLDPDLTNILASSRSYA
MLLFAWEGWHNAAGIPLKPLYEDFTALSNEAYKQDGFTDTGAYWRSWYNS
PTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDRYINLRGPIPAHLLG
DMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWQATHMFRVAEEFFTSL
ELSPMPPEFWEGSMLEKPADGREVVCHASAWDFYNRKDFRIKQCTRVTMD
QLSTVHHEMGHIQYYLQYKDLPVSLRRGANPGFHEAIGDVLALSVSTPEH
LHKIGLLDRVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRT
PPSRYNFDWWYLRTKYQGICPPVTRNETHFDAGAKFHVPNVTPYIRYFVS
FVLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKLRKVLRAGSSRPWQE
VLKDMVGLDALDAQPLLKYFQLVTQWLQEQNQQNGEVLGWPEYQWHPPLP
DNYPE
3D structure
PDB6f9v Crystal structures of sampatrilat and sampatrilat-Asp in complex with human ACE - a molecular basis for domain selectivity.
ChainA
Resolution1.69 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H331 A332 H361 E362 H365 E389 H491 Y501
Catalytic site (residue number reindexed from 1) H327 A328 H357 E358 H361 E385 H487 Y497
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 H361 H365 E389 H357 H361 E385
BS02 D0Z A Q259 H331 A332 S333 A334 H361 E362 H365 H388 E389 K489 H491 Y498 Y501 F505 Q255 H327 A328 S329 A330 H357 E358 H361 H384 E385 K485 H487 Y494 Y497 F501 MOAD: Ki=171.9nM
PDBbind-CN: -logKd/Ki=6.76,Ki=171.9nM
BindingDB: Ki=14nM
BS03 MG A E262 N263 D354 E258 N259 D350
BS04 MG A E262 D354 E258 D350
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:6f9v, PDBe:6f9v, PDBj:6f9v
PDBsum6f9v
PubMed29476645
UniProtP12821|ACE_HUMAN Angiotensin-converting enzyme (Gene Name=ACE)

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