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2P1R

Crystal structure of Salmonella typhimurium YegS, a putative lipid kinase homologous to eukaryotic sphingosine and diacylglycerol kinases.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0001727molecular_functionlipid kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006629biological_processlipid metabolic process
A0006665biological_processsphingolipid metabolic process
A0008654biological_processphospholipid biosynthetic process
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0001727molecular_functionlipid kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006629biological_processlipid metabolic process
B0006665biological_processsphingolipid metabolic process
B0008654biological_processphospholipid biosynthetic process
B0016020cellular_componentmembrane
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016740molecular_functiontransferase activity
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0001727molecular_functionlipid kinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006629biological_processlipid metabolic process
C0006665biological_processsphingolipid metabolic process
C0008654biological_processphospholipid biosynthetic process
C0016020cellular_componentmembrane
C0016301molecular_functionkinase activity
C0016310biological_processphosphorylation
C0016740molecular_functiontransferase activity
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0001727molecular_functionlipid kinase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0006629biological_processlipid metabolic process
D0006665biological_processsphingolipid metabolic process
D0008654biological_processphospholipid biosynthetic process
D0016020cellular_componentmembrane
D0016301molecular_functionkinase activity
D0016310biological_processphosphorylation
D0016740molecular_functiontransferase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 300
ChainResidue
AASP67
AILE70
AASN97
APHE99
AALA100
AHOH305

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 301
ChainResidue
AASP218
ALEU220
AASP125
AASN200
ALEU215

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 302
ChainResidue
ASER242
AASP243
AASN245
AILE248

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 300
ChainResidue
BASP67
BILE70
BASN97
BPHE99
BALA100
BHOH339

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 301
ChainResidue
BASP125
BASN200
BLEU215
BASP218
BLEU220

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 302
ChainResidue
BSER242
BASP243
BASN245
BILE248

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA C 300
ChainResidue
CASP125
CASN200
CLEU215
CASP218
CLEU220

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA C 301
ChainResidue
CSER242
CASP243
CASN245
CILE248

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA C 302
ChainResidue
BGLY94
CARG81
CGLY83
CHOH400

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL C 303
ChainResidue
CASN12
CGLY66
CTHR69
CHOH351

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA D 300
ChainResidue
DASP125
DASN200
DLEU215
DASP218
DLEU220

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA D 301
ChainResidue
DSER242
DASP243
DASN245
DILE248

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA D 302
ChainResidue
AGLY94
DARG81
DGLY83
DHOH382

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL D 303
ChainResidue
DGLY66
DTHR69
DHOH322

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues32
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues36
DetailsBinding site: {}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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