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2IC8

Crystal structure of GlpG

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
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
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

218853

PDB entries from 2024-04-24

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