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3EEB

Structure of the V. cholerae RTX cysteine protease domain

Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE IHP A 210
ChainResidue
AGLU27
AARG182
ALYS183
ALYS195
ALYS200
ANA211
AHOH212
AHOH275
AHOH276
AHOH277
AHOH278
ATHR28
AHOH279
AHOH281
AHOH285
AHOH286
AHOH288
AHOH303
AARG29
ALYS54
AHIS55
AARG85
ASER136
ASER169
AARG171

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 211
ChainResidue
AGLU27
AIHP210
AHOH284
AHOH286

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE IHP B 210
ChainResidue
BGLY25
BGLU27
BTHR28
BARG29
BLYS54
BHIS55
BARG85
BSER136
BSER169
BARG171
BARG182
BLYS183
BLYS195
BLYS200
BNA211
BHOH214
BHOH215
BHOH220
BHOH231
BHOH243
BHOH248
BHOH283
BHOH298
BHOH321
BHOH322

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B 211
ChainResidue
BGLU27
BIHP210
BHOH283
BHOH293

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: For cysteine protease activity => ECO:0000255|PROSITE-ProRule:PRU01107, ECO:0000269|PubMed:17698571
ChainResidueDetails
AHIS91
BHIS91

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile; for cysteine protease activity => ECO:0000255|PROSITE-ProRule:PRU01107, ECO:0000269|PubMed:17698571
ChainResidueDetails
ACYS140
BCYS140

site_idSWS_FT_FI3
Number of Residues16
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
ALYS54
AARG85
ASER136
ASER169
AARG182
ALYS195
ALYS200
BGLU27

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PDB entries from 2024-09-11

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