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2FEP

Structure of truncated CcpA in complex with P-Ser-HPr and Sulfate ions

Functional Information from GO Data
ChainGOidnamespacecontents
S0005515molecular_functionprotein binding
S0005737cellular_componentcytoplasm
S0009401biological_processphosphoenolpyruvate-dependent sugar phosphotransferase system
S0043610biological_processregulation of carbohydrate utilization
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 S 4398
ChainResidue
SASP32
SASN43
SLYS45

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 4397
ChainResidue
APHE75
ATYR76
ATYR222
AHOH4467

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 4396
ChainResidue
AASP249
APHE275
AASP276
ATHR278
AHOH4427
APHE75
ATHR248

Functional Information from PROSITE/UniProt
site_idPS00012
Number of Residues16
DetailsPHOSPHOPANTETHEINE Phosphopantetheine attachment site. TVNLKSIMGVMSLGIA
ChainResidueDetails
STHR41-ALA56

site_idPS00369
Number of Residues8
DetailsPTS_HPR_HIS PTS HPR domain histidine phosphorylation site signature. GIHARPAT
ChainResidueDetails
SGLY13-THR20

site_idPS00589
Number of Residues16
DetailsPTS_HPR_SER PTS HPR domain serine phosphorylation site signature. GKtVNlKSIMGVMsLG
ChainResidueDetails
SGLY39-GLY54

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Pros-phosphohistidine intermediate; alternate => ECO:0000255|PROSITE-ProRule:PRU00681, ECO:0000269|PubMed:1549615
ChainResidueDetails
SALA16

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:17218307
ChainResidueDetails
SGLY13

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Tele-phosphohistidine; alternate => ECO:0000269|PubMed:1549615
ChainResidueDetails
SALA16

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine; by HPrK/P => ECO:0000255|PROSITE-ProRule:PRU00681, ECO:0000269|PubMed:17218307
ChainResidueDetails
SILE47

224201

PDB entries from 2024-08-28

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