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8AB5

Structure of E. coli GlpG in complex with peptide derived inhibitor Ac-VRHA-conh-[4-(4-butyl)-phenoxy-1-phenyl-2-butyl]

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
B0016020cellular_componentmembrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsTRANSMEM: Helical; Name=1 => ECO:0000305
ChainResidueDetails
AGLY94-LEU114
BGLY94-LEU114

site_idSWS_FT_FI2
Number of Residues60
DetailsTOPO_DOM: Periplasmic => ECO:0000305
ChainResidueDetails
AGLY115-HIS141
AGLN190-LYS191
AGLY246-MET249
BGLY115-HIS141
BGLN190-LYS191
BGLY246-MET249

site_idSWS_FT_FI3
Number of Residues40
DetailsTRANSMEM: Helical; Name=2 => ECO:0000305
ChainResidueDetails
AALA142-GLY162
BALA142-GLY162

site_idSWS_FT_FI4
Number of Residues28
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
AGLY163-ARG168
ALEU213-GLY222
BGLY163-ARG168
BLEU213-GLY222

site_idSWS_FT_FI5
Number of Residues40
DetailsTRANSMEM: Helical; Name=3 => ECO:0000305
ChainResidueDetails
ALEU169-GLN189
BLEU169-GLN189

site_idSWS_FT_FI6
Number of Residues40
DetailsTRANSMEM: Helical; Name=4 => ECO:0000305
ChainResidueDetails
APHE192-TRP212
BPHE192-TRP212

site_idSWS_FT_FI7
Number of Residues44
DetailsTRANSMEM: Helical; Name=5 => ECO:0000305
ChainResidueDetails
AILE223-PHE245
BILE223-PHE245

site_idSWS_FT_FI8
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:17051161, ECO:0000305|PubMed:17099694, ECO:0000305|PubMed:17190827, ECO:0000305|PubMed:17277078
ChainResidueDetails
ASER201
BSER201

site_idSWS_FT_FI9
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:17051161, ECO:0000305|PubMed:17099694, ECO:0000305|PubMed:17190827, ECO:0000305|PubMed:17277078
ChainResidueDetails
AHIS254
BHIS254

219869

PDB entries from 2024-05-15

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