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1UZE

Complex of the anti-hypertensive drug enalaprilat and the human testicular angiotensin I-converting enzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008241molecular_functionpeptidyl-dipeptidase activity
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 701
ChainResidue
AHIS383
AHIS387
AGLU411
AEAL3002

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 703
ChainResidue
AARG186
ATRP485
ATRP486
AARG489

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 704
ChainResidue
APRO407
APRO519
AILE521
AARG522
AHOH2172
ATYR224

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GLY A2000
ChainResidue
AVAL379
AASP415
AASP453
ALYS454
APHE527
AHOH2334
AEAL3002

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE EAL A3002
ChainResidue
AGLN281
AHIS353
AALA354
AHIS383
AGLU384
AHIS387
AGLU411
ALYS511
APHE512
AHIS513
AVAL518
ATYR520
ATYR523
AZN701
AGLY2000
AHOH2281
AHOH2455
AHOH2456

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAHHEMGHIQ
ChainResidueDetails
AVAL380-GLN389

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor 1 => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:12540854, ECO:0000305|PubMed:16154999, ECO:0000305|PubMed:19773553
ChainResidueDetails
ATYR360

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor 1 => ECO:0000255|PROSITE-ProRule:PRU01355
ChainResidueDetails
AARG489

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton acceptor 2 => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:12540854, ECO:0000305|PubMed:16154999, ECO:0000305|PubMed:19773553
ChainResidueDetails
AGLU384

site_idSWS_FT_FI4
Number of Residues1
DetailsACT_SITE: Proton donor 2 => ECO:0000255|PROSITE-ProRule:PRU01355
ChainResidueDetails
AHIS513

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:16476442
ChainResidueDetails
ATYR200
APRO498

site_idSWS_FT_FI6
Number of Residues2
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
APHE359
ALYS363

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:12540854, ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:23056909, ECO:0007744|PDB:4APH
ChainResidueDetails
AHIS387
AHIS383

site_idSWS_FT_FI8
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:12540854
ChainResidueDetails
AARG186
ATYR224
ATRP485
AARG489

site_idSWS_FT_FI9
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:12540854, ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:23056909, ECO:0000269|PubMed:7961923, ECO:0007744|PDB:4APH
ChainResidueDetails
AGLU411

site_idSWS_FT_FI10
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:12540854, ECO:0000305|PubMed:11432860
ChainResidueDetails
AARG522

site_idSWS_FT_FI11
Number of Residues1
DetailsSITE: Not glycosylated => ECO:0000269|PubMed:20826823
ChainResidueDetails
ATYR492

site_idSWS_FT_FI12
Number of Residues1
DetailsSITE: Cleavage => ECO:0000269|PubMed:7499427, ECO:0000269|PubMed:8253769
ChainResidueDetails
AARG561

site_idSWS_FT_FI13
Number of Residues1
DetailsSITE: Not glycosylated => ECO:0000269|PubMed:9013598
ChainResidueDetails
AASN620

site_idSWS_FT_FI14
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:26403559, ECO:0007744|PDB:3NXQ
ChainResidueDetails
AGLU43

site_idSWS_FT_FI15
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:9013598
ChainResidueDetails
AILE80

site_idSWS_FT_FI16
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:9013598
ChainResidueDetails
AILE115

site_idSWS_FT_FI17
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20826823
ChainResidueDetails
AALA129

site_idSWS_FT_FI18
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16476442
ChainResidueDetails
ATYR287

site_idSWS_FT_FI19
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:26403559, ECO:0007744|PDB:3NXQ
ChainResidueDetails
AGLY414

site_idSWS_FT_FI20
Number of Residues1
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
ALYS478

site_idSWS_FT_FI21
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23056909, ECO:0007744|PDB:4APH
ChainResidueDetails
AASN72

site_idSWS_FT_FI22
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:9013598
ChainResidueDetails
AASN90

site_idSWS_FT_FI23
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:23056909, ECO:0000269|PubMed:9013598, ECO:0007744|PDB:4APH
ChainResidueDetails
AASN109

site_idSWS_FT_FI24
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:9013598
ChainResidueDetails
AASN155
AASN337
AASN586

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1i1i
ChainResidueDetails
ATYR523
AGLU411

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1i1i
ChainResidueDetails
AGLU384
AHIS353
AHIS513
AALA354
ATYR523

site_idMCSA1
Number of Residues8
DetailsM-CSA 170
ChainResidueDetails
AHIS353electrostatic stabiliser, hydrogen bond acceptor
AALA354electrostatic stabiliser, hydrogen bond acceptor
AHIS383metal ligand
AGLU384electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS387metal ligand
AGLU411metal ligand
AHIS513electrostatic stabiliser, hydrogen bond donor
ATYR523electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-11-06

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