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2BON

Structure of an Escherichia coli lipid kinase (YegS)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0001727molecular_functionlipid kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0008654biological_processphospholipid biosynthetic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0001727molecular_functionlipid kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0008654biological_processphospholipid biosynthetic process
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A1302
ChainResidue
ALEU215
AASP218
ALEU220
AHOH2007
AHOH2018
AHOH2024

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B1302
ChainResidue
BHOH2025
BHOH2026
BHOH2030
BLEU215
BASP218
BLEU220

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AGLU271
BGLU271

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ATHR40
AGLY66
ATHR95
BTHR40
BGLY66
BTHR95

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:17351295
ChainResidueDetails
ALEU215
AASP218
ALEU220
BLEU215
BASP218
BLEU220

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PDB entries from 2024-08-14

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