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6XRO

Crystal structure of GlpG in complex with peptide boronate inhibitor, Ac-KRFRSMQYSA-B(OH)2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue B2A B 501
ChainResidue
AGLY198
ANA304
AHOH623
BSER500
AGLY199
ALEU200
ASER201
AGLY202
AALA250
AALA253
AHIS254
ANA303

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 301
ChainResidue
AGLN189
ASER193
AASN251

site_idAC3
Number of Residues5
Detailsbinding site for residue CL A 302
ChainResidue
AARG92
AALA93
ATRP159
AGLN226
AGLY228

site_idAC4
Number of Residues6
Detailsbinding site for residue NA A 303
ChainResidue
ASER201
AMET249
AHIS254
BB2A501
AHOH622
AHOH630

site_idAC5
Number of Residues4
Detailsbinding site for residue NA A 304
ChainResidue
AHIS150
AASN154
BB2A501
AHOH636

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 Residues17
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
AGLY163-ARG168
ALEU213-GLY222
AARG273-LYS276

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
ASER201

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

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PDB entries from 2024-07-24

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