Structure of PDB 6qs1 Chain A

Receptor sequence
>6qs1A (length=608) Species: 9606 (Homo sapiens) [Search protein sequence]
LDPGLQPGQFSADEAGAQLFAQSYQSSAEQVLFQSVAASWAHDTNITAEN
ARRQEEAALLSQEFAEAWGQKAKELYEPIWQQFTDPQLRRIIGAVRTLGS
ANLPLAKRQQYNALLSQMSRIYSTAKVCLATCWSLDPDLTNILASSRSYA
MLLFAWEGWHNAAGIPLKPLYEDFTALSNEAYKQDGFTDTGAYWRSWYNS
PTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDRYINLRGPIPAHLLG
DMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWQATHMFRVAEEFFTSL
ELSPMPPEFWEGSMLEKPADGREVVCHASAWDFYNRKDFRIKQCTRVTMD
QLSTVHHEMGHIQYYLQYKDLPVSLRRGANPGFHEAIGDVLALSVSTPEH
LHKIGLLDRVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRT
PPSRYNFDWWYLRTKYQGICPPVTRNETHFDAGAKFHVPNVTPYIRYFVS
FVLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKLRKVLRAGSSRPWQE
VLKDMVGLDALDAQPLLKYFQLVTQWLQEQNQQNGEVLGWPEYQWHPPLP
DNYPEGID
3D structure
PDB6qs1 Structural basis for the C-domain-selective angiotensin-converting enzyme inhibition by bradykinin-potentiating peptide b (BPPb).
ChainA
Resolution1.8 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
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:6qs1, PDBe:6qs1, PDBj:6qs1
PDBsum6qs1
PubMed31072910
UniProtP12821|ACE_HUMAN Angiotensin-converting enzyme (Gene Name=ACE)

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