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3D8V

Crystal structure of GlmU from Mycobacterium tuberculosis in complex with uridine-diphosphate-N-acetylglucosamine

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
A0035635biological_processentry of bacterium into host cell
A0044650biological_processadhesion of symbiont to host cell
A0046872molecular_functionmetal ion binding
A0070569molecular_functionuridylyltransferase activity
A0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE UD1 A 496
ChainResidue
ALEU12
ASER112
ATYR150
AGLY151
AGLU166
AASN181
ATHR211
AASN239
AHOH497
AHOH517
AHOH586
AALA14
AGLY15
AGLN83
APRO86
ALEU87
AGLY88
ATHR89
AALA92

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues239
DetailsRegion: {"description":"Pyrophosphorylase","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsRegion: {"description":"Linker","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"JUL-2011","submissionDatabase":"PDB data bank","title":"Structure of Mycobacterium tuberculosis GlmU in complex with Acetyl CoA.","authors":["Jagtap P.A.","Prakash B."]}}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19237750","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23485416","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2011","submissionDatabase":"PDB data bank","title":"Structure of Mycobacterium tuberculosis GlmU in complex with Acetyl CoA.","authors":["Jagtap P.A.","Prakash B."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2012","submissionDatabase":"PDB data bank","title":"Structural snapshots of Glmu from Mycobacterium tuberculosis.","authors":["Jagtap P.A.","Verma S.K.","Prakash B."]}}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2012","submissionDatabase":"PDB data bank","title":"Structural snapshots of Glmu from Mycobacterium tuberculosis.","authors":["Jagtap P.A.","Verma S.K.","Prakash B."]}}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19237750","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2011","submissionDatabase":"PDB data bank","title":"Structure of Mycobacterium tuberculosis GlmU in complex with Acetyl CoA.","authors":["Jagtap P.A.","Prakash B."]}}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19237750","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23485416","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2012","submissionDatabase":"PDB data bank","title":"Structural snapshots of Glmu from Mycobacterium tuberculosis.","authors":["Jagtap P.A.","Verma S.K.","Prakash B."]}}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19121323","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23485416","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2011","submissionDatabase":"PDB data bank","title":"Structure of Mycobacterium tuberculosis GlmU in complex with Acetyl CoA.","authors":["Jagtap P.A.","Prakash B."]}},{"source":"PDB","id":"3SPT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HCQ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23485416","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2012","submissionDatabase":"PDB data bank","title":"Structural snapshots of Glmu from Mycobacterium tuberculosis.","authors":["Jagtap P.A.","Verma S.K.","Prakash B."]}}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2011","submissionDatabase":"PDB data bank","title":"Structure of Mycobacterium tuberculosis GlmU in complex with Acetyl CoA.","authors":["Jagtap P.A.","Prakash B."]}}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2011","submissionDatabase":"PDB data bank","title":"Structure of Mycobacterium tuberculosis GlmU in complex with Acetyl CoA.","authors":["Jagtap P.A.","Prakash B."]}}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"N-acetylthreonine","evidences":[{"source":"PubMed","id":"21969609","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsCross-link: {"description":"Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)","evidences":[{"source":"PubMed","id":"20066036","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1lxa
ChainResidueDetails
AGLU385

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1lxa
ChainResidueDetails
AARG19

238582

PDB entries from 2025-07-09

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