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3GCD

Structure of the V. cholerae RTX cysteine protease domain in complex with an aza-Leucine peptide inhibitor

Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AZ0 A 213
ChainResidue
AVAL43
ALEU175
AALA176
AVAL177
AHIS184
AHOH220
AALA47
AASN50
AGLY90
AHIS91
AGLY92
AVAL138
ACYS140
AGLU174

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE IHP A 214
ChainResidue
AGLU27
ATHR28
AARG29
APHE30
ALYS54
AHIS55
AARG85
ASER136
ASER169
AARG171
AARG182
ALYS183
ALYS195
ALYS200
ANA215
AHOH221
AHOH223
AHOH229
AHOH230
AHOH249
AHOH251
AHOH253

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 215
ChainResidue
AGLU27
AIHP214
AHOH252

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AZ0 B 213
ChainResidue
AHIS95
BVAL43
BALA47
BASN50
BGLY90
BHIS91
BGLY92
BCYS140
BLEU175
BALA176
BVAL177
BTRP192
BHOH240

site_idAC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE IHP B 214
ChainResidue
BGLU27
BTHR28
BARG29
BLYS54
BHIS55
BARG85
BHIS134
BSER136
BSER169
BARG171
BARG182
BLYS183
BLYS195
BLYS200
BNA215

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA B 215
ChainResidue
BGLU27
BIHP214

site_idAC7
Number of Residues21
DetailsBINDING SITE FOR RESIDUE AZ0 C 213
ChainResidue
BASP109
BASN157
BALA158
CLYS4
CVAL43
CLYS46
CALA47
CASN50
CGLY90
CHIS91
CGLY92
CVAL138
CCYS140
CGLU174
CLEU175
CALA176
CVAL177
CTRP192
CHOH230
CHOH244
DARG165

site_idAC8
Number of Residues19
DetailsBINDING SITE FOR RESIDUE IHP C 214
ChainResidue
CARG182
CLYS183
CLYS195
CLYS200
CNA215
CHOH217
CHOH219
CHOH220
CHOH235
CHOH254
CGLU27
CTHR28
CARG29
CLYS54
CHIS55
CARG85
CSER136
CSER169
CARG171

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA C 215
ChainResidue
CGLU27
CIHP214
CHOH240
CHOH254

site_idBC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE AZ0 D 213
ChainResidue
DLYS4
DVAL43
DALA47
DASN50
DGLY90
DHIS91
DGLY92
DHIS95
DGLU97
DASN100
DCYS140
DLEU175
DALA176
DVAL177
DTRP192
DHOH227

site_idBC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE IHP D 214
ChainResidue
DTHR28
DARG29
DLYS54
DHIS55
DARG85
DSER136
DSER169
DARG171
DARG182
DLYS183
DLYS195
DLYS200
DNA215
DHOH218

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA D 215
ChainResidue
DGLU27
DIHP214

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: For cysteine protease activity => ECO:0000255|PROSITE-ProRule:PRU01107, ECO:0000269|PubMed:17698571
ChainResidueDetails
AHIS91
BHIS91
CHIS91
DHIS91

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Nucleophile; for cysteine protease activity => ECO:0000255|PROSITE-ProRule:PRU01107, ECO:0000269|PubMed:17698571
ChainResidueDetails
ACYS140
BCYS140
CCYS140
DCYS140

site_idSWS_FT_FI3
Number of Residues32
DetailsBINDING: BINDING => ECO:0000269|PubMed:18845756, ECO:0000269|PubMed:19465933, ECO:0000269|PubMed:19620709, ECO:0007744|PDB:3EEB, ECO:0007744|PDB:3FZY, ECO:0007744|PDB:3GCD
ChainResidueDetails
AGLU27
BLYS54
BARG85
BSER136
BSER169
BARG182
BLYS195
BLYS200
CGLU27
CLYS54
CARG85
ALYS54
CSER136
CSER169
CARG182
CLYS195
CLYS200
DGLU27
DLYS54
DARG85
DSER136
DSER169
AARG85
DARG182
DLYS195
DLYS200
ASER136
ASER169
AARG182
ALYS195
ALYS200
BGLU27

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PDB entries from 2024-10-09

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