Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2XTV

Structure of E.coli rhomboid protease GlpG, active site mutant, S201T, orthorhombic crystal form

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MC3 A 501
ChainResidue
ATHR130
AMC3505
AHOH2076
APHE133
AGLU134
APHE135
ATRP136
AARG217
AALA263
APHE266
AMC3503

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MC3 A 502
ChainResidue
ATRP122
APHE153
ALEU156
ATRP157
ATRP159
ATYR160
AGLN226
APHE232
APHE245
AHOH2077

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MC3 A 503
ChainResidue
ATRP136
APHE153
ALEU155
ALEU156
ATRP159
APHE266
ALEU270
AMC3501
AMC3509
AMC3511
AHOH2079

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MC3 A 504
ChainResidue
ALEU184
AALA256
AALA263
AMC3512

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MC3 A 505
ChainResidue
ALYS132
ATYR138
ATRP212
AGLU216
AMC3501
AMC3506
AMC3507
AMC3508

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MC3 A 506
ChainResidue
AVAL106
AILE109
ALEU234
AMC3505
AMC3508
AMC3512

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MC3 A 507
ChainResidue
ATRP125
ALEU183
AGLN190
AMC3505
AMC3508

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MC3 A 508
ChainResidue
ATYR187
AMC3505
AMC3506
AMC3507

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MC3 A 509
ChainResidue
APHE139
AILE175
ALEU179
AMC3503
AMC3510

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MC3 A 510
ChainResidue
AMC3509

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MC3 A 511
ChainResidue
AGLN112
AMC3503
AMC3512

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MC3 A 512
ChainResidue
ATYR187
AMC3504
AMC3506
AMC3511

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MC3 A 513
ChainResidue
APHE242
AVAL267
AASN271

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MC3 A 514
ChainResidue
AILE102
APHE242
AASP243

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsTRANSMEM: Helical; Name=1 => ECO:0000305
ChainResidueDetails
AGLY94-LEU114

site_idSWS_FT_FI2
Number of Residues30
DetailsTOPO_DOM: Periplasmic => ECO:0000305
ChainResidueDetails
AGLY115-HIS141
AGLN190-LYS191
AGLY246-MET249

site_idSWS_FT_FI3
Number of Residues20
DetailsTRANSMEM: Helical; Name=2 => ECO:0000305
ChainResidueDetails
AALA142-GLY162

site_idSWS_FT_FI4
Number of Residues14
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
AGLY163-ARG168
ALEU213-GLY222

site_idSWS_FT_FI5
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000305
ChainResidueDetails
ALEU169-GLN189

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000305
ChainResidueDetails
APHE192-TRP212

site_idSWS_FT_FI7
Number of Residues22
DetailsTRANSMEM: Helical; Name=5 => ECO:0000305
ChainResidueDetails
AILE223-PHE245

site_idSWS_FT_FI8
Number of Residues22
DetailsTRANSMEM: Helical; Name=6 => ECO:0000305
ChainResidueDetails
AALA250-ALA272

site_idSWS_FT_FI9
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:17051161, ECO:0000305|PubMed:17099694, ECO:0000305|PubMed:17190827, ECO:0000305|PubMed:17277078
ChainResidueDetails
ATHR201

site_idSWS_FT_FI10
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:17051161, ECO:0000305|PubMed:17099694, ECO:0000305|PubMed:17190827, ECO:0000305|PubMed:17277078
ChainResidueDetails
AHIS254

220113

PDB entries from 2024-05-22

PDB statisticsPDBj update infoContact PDBjnumon