Structure of PDB 6qs1 Chain B

Receptor sequence
>6qs1B (length=603) Species: 9606 (Homo sapiens) [Search protein sequence]
LDPGLQPGQFSADEAGAQLFAQSYQSSAEQVLFQSVAASWAHDTNITAEN
ARRQEEAALLSQEFAEAWGQKAKELYEPIWQQFTDPQLRRIIGAVRTLGS
ANLPLAKRQQYNALLSQMSRIYSTAKVCLTCWSLDPDLTNILASSRSYAM
LLFAWEGWHNAAGIPLKPLYEDFTALSNEAYKQDGFTDTGAYWRSWYNSP
TFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDRYINLRGPIPAHLLGD
MWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWQATHMFRVAEEFFTSLE
LSPMPPEFWEGSMLEKPADGREVVCHASAWDFYNRKDFRIKQCTRVTMDQ
LSTVHHEMGHIQYYLQYKDLPVSLRRGANPGFHEAIGDVLALSVSTPEHL
HKIGLLDRVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTP
PSRYNFDWWYLRTKYQGICPPVTRNETHFDAGAKFHVPNVTPYIRYFVSF
VLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKLRKVLRAGSSRPWQEV
LKDMVGLDALDAQPLLKYFQLVTQWLQEQNQQNGEVLGWPEYQWHPPLPD
NYP
3D structure
PDB6qs1 Structural basis for the C-domain-selective angiotensin-converting enzyme inhibition by bradykinin-potentiating peptide b (BPPb).
ChainB
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) H326 A327 H356 E357 H360 E384 H486 Y496
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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