Structure of PDB 8qfx Chain D

Receptor sequence
>8qfxD (length=605) Species: 9606 (Homo sapiens) [Search protein sequence]
LDPGLQPGQFSADEAGAQLFAQSYQSSAEQVLFQSVAASWAHDTNITAEN
ARRQEEAALLSQEFAEAWGQKAKELYEPIWQQFTDPQLRRIIGAVRTLGS
ANLPLAKRQQYNALLSQMSRIYSTAKVCLPQTCWSLDPDLTNILASSRSY
AMLLFAWEGWHNAAGIPLKPLYEDFTALSNEAYKQDGFTDTGAYWRSWYN
SPTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDRYINLRGPIPAHLL
GDMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWQATHMFRVAEEFFTS
LELSPMPPEFWEGSMLEKPADGREVVCHASAWDFYNRKDFRIKQCTRVTM
DQLSTVHHEMGHIQYYLQYKDLPVSLRRGANPGFHEAIGDVLALSVSTPE
HLHKIGLLDRVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFSGR
TPPSRYNFDWWYLRTKYQGICPPVTRNETHFDAGAKFHVPNVTPYIRYFV
SFVLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKLRKVLRAGSSRPWQ
EVLKDMVGLDALDAQPLLKYFQLVTQWLQEQNQQNGEVLGWPEYQWHPPL
PDNYP
3D structure
PDB8qfx Structural insights into the inhibitory mechanism of angiotensin-I-converting enzyme by the lactotripeptides IPP and VPP.
ChainD
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 D Q259 H331 A332 H361 E362 H365 F435 K489 H491 Y498 Y501 Q256 H328 A329 H358 E359 H362 F432 K486 H488 Y495 Y498
BS02 ZN D H361 H365 E389 H358 H362 E386
BS03 MG D E262 D354 E259 D351
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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