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6QS1

Crystal structure of human Angiotensin-1 converting enzyme N-domain in complex with BPPb

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008241molecular_functionpeptidyl-dipeptidase activity
A0016020cellular_componentmembrane
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0008241molecular_functionpeptidyl-dipeptidase activity
B0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TVHHEMGHIQ
ChainResidueDetails
ATHR358-GLN367

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor 1 => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:12540854, ECO:0000305|PubMed:16154999, ECO:0000305|PubMed:19773553
ChainResidueDetails
AGLU362
BGLU362

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor 1 => ECO:0000255|PROSITE-ProRule:PRU01355
ChainResidueDetails
AHIS491
BHIS491

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:16476442
ChainResidueDetails
ATYR202
AARG500
BTYR202
BARG500

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:26403559, ECO:0007744|PDB:2OC2, ECO:0007744|PDB:3NXQ
ChainResidueDetails
AHIS361
AHIS365
AGLU389
BHIS361
BHIS365
BGLU389

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Not glycosylated => ECO:0000269|PubMed:20826823
ChainResidueDetails
AASN494
BASN494

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20826823, ECO:0000305|PubMed:9013598
ChainResidueDetails
AGLN9
BGLN9

site_idSWS_FT_FI7
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:9013598
ChainResidueDetails
AGLN25
AGLN117
BGLN25
BGLN117

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:26403559, ECO:0007744|PDB:3NXQ
ChainResidueDetails
AASN45
BASN45

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:9013598
ChainResidueDetails
AGLN82
BGLN82

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20826823
ChainResidueDetails
AGLN131
BGLN131

site_idSWS_FT_FI11
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16476442
ChainResidueDetails
AGLN289
BGLN289

site_idSWS_FT_FI12
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:26403559, ECO:0007744|PDB:3NXQ
ChainResidueDetails
AASN416
BASN416

site_idSWS_FT_FI13
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:26403559, ECO:0000269|PubMed:9013598, ECO:0007744|PDB:3NXQ
ChainResidueDetails
AASN480
BASN480

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 170
ChainResidueDetails

site_idMCSA2
Number of Residues
DetailsM-CSA 170
ChainResidueDetails

226707

PDB entries from 2024-10-30

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