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6VU0

CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF ENZYME I OF THE BACTERIAL PHOSPHOTRANSFERASE SYSTEM FROM THE ESCHERICHIA COLI ENZYME

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0016310biological_processphosphorylation
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
B0003824molecular_functioncatalytic activity
B0016310biological_processphosphorylation
B0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue SO4 A 600
ChainResidue
AARG296
AARG332

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 B 601
ChainResidue
BARG296
BARG332
BASN454

Functional Information from PROSITE/UniProt
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":"Proton donor","evidences":[{"source":"PubMed","id":"12705838","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17053069","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P23533","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17053069","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 920
ChainResidueDetails
AGLU431metal ligand
AASP455metal ligand
ACYS502proton shuttle (general acid/base)

site_idMCSA2
Number of Residues3
DetailsM-CSA 920
ChainResidueDetails
BGLU431metal ligand
BASP455metal ligand
BCYS502proton shuttle (general acid/base)

242842

PDB entries from 2025-10-08

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