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5T91

Crystal structure of B. subtilis 168 GlpQ in complex with bicine

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0006071biological_processglycerol metabolic process
A0006629biological_processlipid metabolic process
A0008081molecular_functionphosphoric diester hydrolase activity
A0008889molecular_functionglycerophosphodiester phosphodiesterase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CA A 301
ChainResidue
AHIS43
AGLU70
ABCN302
AHOH420

site_idAC2
Number of Residues12
Detailsbinding site for residue BCN A 302
ChainResidue
AGLN188
APHE190
ATYR259
APHE279
ACA301
AHOH420
AHOH514
AHIS43
AARG44
AGLU70
AASP72
AHIS85

site_idAC3
Number of Residues6
Detailsbinding site for residue NA A 303
ChainResidue
AASP90
ATHR93
AHOH445
AHOH534
AHOH582
AHOH589

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"27780866","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"27780866","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27780866","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5T9B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5T9C","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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