Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2HRO

Structure of the full-lenght Enzyme I of the PTS system from Staphylococcus carnosus

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0008965molecular_functionphosphoenolpyruvate-protein phosphotransferase activity
A0009401biological_processphosphoenolpyruvate-dependent sugar phosphotransferase system
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 900
ChainResidue
AARG297
AARG333
AASN455
AARG466

Functional Information from PROSITE/UniProt
site_idPS00370
Number of Residues12
DetailsPEP_ENZYMES_PHOS_SITE PEP-utilizing enzymes phosphorylation site signature. GGrTsHSAIMSR
ChainResidueDetails
AGLY185-ARG196

site_idPS00742
Number of Residues19
DetailsPEP_ENZYMES_2 PEP-utilizing enzymes signature 2. DfFSIGTNDLiQYTMAadR
ChainResidueDetails
AASP448-ARG466

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Tele-phosphohistidine intermediate => ECO:0000250|UniProtKB:P08839, ECO:0000305|PubMed:16867985
ChainResidueDetails
AHIS190

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P08839, ECO:0000305|PubMed:16867985
ChainResidueDetails
ACYS503

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16867985
ChainResidueDetails
AARG297
AARG333
AASN455
AARG466

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P08839
ChainResidueDetails
AGLU432
AASP456

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1kc7
ChainResidueDetails
ACYS503
AHIS190

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1kc7
ChainResidueDetails
ATHR169
AHIS190

224201

PDB entries from 2024-08-28

PDB statisticsPDBj update infoContact PDBjnumon