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2OI7

E. coli GlmU- Complex with UDP-GlcNAc, desulpho-CoA and GlcNAc-1-PO4

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0000902biological_processcell morphogenesis
A0003824molecular_functioncatalytic activity
A0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006048biological_processUDP-N-acetylglucosamine biosynthetic process
A0008360biological_processregulation of cell shape
A0009245biological_processlipid A biosynthetic process
A0009252biological_processpeptidoglycan biosynthetic process
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0019134molecular_functionglucosamine-1-phosphate N-acetyltransferase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0071555biological_processcell wall organization
B0000287molecular_functionmagnesium ion binding
B0000902biological_processcell morphogenesis
B0003824molecular_functioncatalytic activity
B0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006048biological_processUDP-N-acetylglucosamine biosynthetic process
B0008360biological_processregulation of cell shape
B0009245biological_processlipid A biosynthetic process
B0009252biological_processpeptidoglycan biosynthetic process
B0016020cellular_componentmembrane
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0016779molecular_functionnucleotidyltransferase activity
B0019134molecular_functionglucosamine-1-phosphate N-acetyltransferase activity
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0071555biological_processcell wall organization
Functional Information from PROSITE/UniProt
site_idPS00101
Number of Residues29
DetailsHEXAPEP_TRANSFERASES Hexapeptide-repeat containing-transferases signature. VGsdTqLvapVtVGkgAtIAagTtVtrnV
ChainResidueDetails
AVAL403-VAL431

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsRegion: {"description":"Linker","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10428949","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8555230","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10428949","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11329257","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17473010","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17473010","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2OI5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11329257","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17473010","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11329257","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17473010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21984832","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17473010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21984832","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1lxa
ChainResidueDetails
AASN386

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1lxa
ChainResidueDetails
BASN386

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1lxa
ChainResidueDetails
AARG18

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1lxa
ChainResidueDetails
BARG18

site_idMCSA1
Number of Residues1
DetailsM-CSA 811
ChainResidueDetails
AARG18electrostatic stabiliser

site_idMCSA2
Number of Residues1
DetailsM-CSA 811
ChainResidueDetails
BARG18electrostatic stabiliser

246031

PDB entries from 2025-12-10

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