Structure of PDB 8qfx Chain A

Receptor sequence
>8qfxA (length=609) Species: 9606 (Homo sapiens) [Search protein sequence]
LDPGLQPGQFSADEAGAQLFAQSYQSSAEQVLFQSVAASWAHDTNITAEN
ARRQEEAALLSQEFAEAWGQKAKELYEPIWQQFTDPQLRRIIGAVRTLGS
ANLPLAKRQQYNALLSQMSRIYSTAKVCLPTCWSLDPDLTNILASSRSYA
MLLFAWEGWHNAAGIPLKPLYEDFTALSNEAYKQDGFTDTGAYWRSWYNS
PTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDRYINLRGPIPAHLLG
DMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWQATHMFRVAEEFFTSL
ELSPMPPEFWEGSMLEKPADGREVVCHASAWDFYNRKDFRIKQCTRVTMD
QLSTVHHEMGHIQYYLQYKDLPVSLRRGANPGFHEAIGDVLALSVSTPEH
LHKIGLLDRVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRT
PPSRYNFDWWYLRTKYQGICPPVTRNETHFDAGAKFHVPNVTPYIRYFVS
FVLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKLRKVLRAGSSRPWQE
VLKDMVGLDALDAQPLLKYFQLVTQWLQEQNQQNGEVLGWPEYQWHPPLP
DNYPEGIDL
3D structure
PDB8qfx Structural insights into the inhibitory mechanism of angiotensin-I-converting enzyme by the lactotripeptides IPP and VPP.
ChainA
Resolution1.6 Å
3D
structure
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Enzymatic activity
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 peptide A Q259 H331 A332 H361 E362 H365 F435 K489 H491 Y498 Y501 Q255 H327 A328 H357 E358 H361 F431 K485 H487 Y494 Y497
BS02 FUC A T478 H483 T474 H479
BS03 ZN A H361 H365 E389 H357 H361 E385
BS04 MG A E262 N263 D354 E258 N259 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:8qfx, PDBe:8qfx, PDBj:8qfx
PDBsum8qfx
PubMed37904282
UniProtP12821|ACE_HUMAN Angiotensin-converting enzyme (Gene Name=ACE)

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