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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4G3Q

Crystal structure of GlmU from Mycobacterium tuberculosis Snapshot 4

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 Residues15
DetailsBINDING SITE FOR RESIDUE POP A 501
ChainResidue
APRO16
AHOH1133
AHOH1134
AHOH1135
AHOH1136
AHOH1143
AHOH1144
AGLY17
ATHR18
AARG19
AMG502
AUD1506
AHOH601
AHOH1033
AHOH1132
site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
APOP501
AHOH1132
AHOH1133
AHOH1134
AHOH1135
site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MG A 503
ChainResidue
AASP417
AASP417
AASP417
ACO505
ACO505
ACO505
AHOH602
AHOH602
AHOH602
site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 504
ChainResidue
AASP114
AASN239
AUD1506
AHOH1137
AHOH1138
site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 505
ChainResidue
AASP417
AASP417
AASP417
AMG503
AMG503
AMG503
site_idAC6
Number of Residues35
DetailsBINDING SITE FOR RESIDUE UD1 A 506
ChainResidue
ALEU12
AALA13
AALA14
AGLY15
AARG19
ALYS26
AGLN83
APRO86
ALEU87
AGLY88
ATHR89
AALA92
ASER112
AGLY113
AASP114
ATYR150
AGLY151
AGLU166
AASN181
AALA182
ATYR209
ATHR211
AASN239
APOP501
ACO504
AHOH624
AHOH643
AHOH670
AHOH791
AHOH1034
AHOH1036
AHOH1133
AHOH1137
AHOH1138
AHOH1143
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsRegion: {"description":"Linker","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
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_FI3
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_FI4
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_FI5
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_FI6
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_FI7
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_FI8
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_FI9
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_FI10
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
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_FI12
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

247536

PDB entries from 2026-01-14

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