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2HWG

Structure of phosphorylated Enzyme I of the phosphoenolpyruvate:sugar phosphotransferase system

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008965molecular_functionphosphoenolpyruvate-protein phosphotransferase activity
A0009401biological_processphosphoenolpyruvate-dependent sugar phosphotransferase system
A0015764biological_processN-acetylglucosamine transport
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008965molecular_functionphosphoenolpyruvate-protein phosphotransferase activity
B0009401biological_processphosphoenolpyruvate-dependent sugar phosphotransferase system
B0015764biological_processN-acetylglucosamine transport
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016740molecular_functiontransferase activity
B0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 901
ChainResidue
ANEP189
AARG358
AGLU431
AASP455
AOXL903
AHOH1001

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 902
ChainResidue
BASP455
BARG465
BOXL904
BHOH1002
BNEP189
BARG358
BGLU431

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE OXL A 903
ChainResidue
ANEP189
AARG296
AARG332
AMSE429
AGLU431
AGLY452
ATHR453
AASN454
AASP455
AARG465
ACYS502
AGLY503
AMG901
AHOH1001

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE OXL B 904
ChainResidue
BNEP189
BARG296
BARG332
BMSE429
BGLU431
BGLY452
BTHR453
BASN454
BASP455
BARG465
BGLY503
BMG902
BHOH1002

Functional Information from PROSITE/UniProt
site_idPS00370
Number of Residues12
DetailsPEP_ENZYMES_PHOS_SITE PEP-utilizing enzymes phosphorylation site signature. GGrTsHTSIMAR
ChainResidueDetails
AGLY184-ARG195

site_idPS00742
Number of Residues19
DetailsPEP_ENZYMES_2 PEP-utilizing enzymes signature 2. DfFSIGTNDLtQYTLAvdR
ChainResidueDetails
AASP447-ARG465

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"PubMed","id":"12705838","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17053069","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"12705838","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17053069","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P23533","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17053069","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"33376208","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1kc7
ChainResidueDetails
ACYS502

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1kc7
ChainResidueDetails
BCYS502

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1kc7
ChainResidueDetails
ATHR168

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1kc7
ChainResidueDetails
BTHR168

site_idMCSA1
Number of Residues4
DetailsM-CSA 920
ChainResidueDetails
AALA201covalent catalysis
AASN483metal ligand
AGLY507metal ligand
AASN566proton shuttle (general acid/base)

site_idMCSA2
Number of Residues4
DetailsM-CSA 920
ChainResidueDetails
BALA201covalent catalysis
BASN483metal ligand
BGLY507metal ligand
BASN566proton shuttle (general acid/base)

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PDB entries from 2025-07-23

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