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4G87

Crystal structure of GLMU from Mycobacterium tuberculosis snapshot 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0000902biological_processcell morphogenesis
A0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0006048biological_processUDP-N-acetylglucosamine biosynthetic process
A0008360biological_processregulation of cell shape
A0009245biological_processlipid A biosynthetic process
A0009252biological_processpeptidoglycan biosynthetic process
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 Residues9
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
AASP417
AASP417
AASP417
ACO503
ACO503
ACO503
AHOH805
AHOH805
AHOH805

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 502
ChainResidue
ALYS26
AASP114
AASN239
AUD1505
AHOH635
AHOH684

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 503
ChainResidue
AASP417
AASP417
AASP417
AMG501
AMG501
AMG501

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 504
ChainResidue
AUD1505
APOP506
AHOH777
AHOH964
AHOH1071

site_idAC5
Number of Residues29
DetailsBINDING SITE FOR RESIDUE UD1 A 505
ChainResidue
ALEU12
AALA13
AALA14
AGLY15
AARG19
ALYS26
AGLN83
APRO86
ALEU87
AGLY88
ATHR89
AALA92
AASP114
ATYR150
AGLY151
AGLU166
AASN181
ATHR211
AASN239
ACO502
AMG504
APOP506
AHOH624
AHOH635
AHOH672
AHOH684
AHOH691
AHOH696
AHOH964

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE POP A 506
ChainResidue
AGLY15
APRO16
AGLY17
ATHR18
AARG19
ALYS26
AMG504
AUD1505
AHOH618
AHOH964
AHOH996
AHOH1071

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000305|Ref.7
ChainResidueDetails
AHIS374

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:19237750, ECO:0000269|PubMed:23485416, ECO:0000269|Ref.7, ECO:0000269|Ref.8
ChainResidueDetails
ALEU12
AGLY88
AGLY151
AGLU166
AASN181
AASN239

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|Ref.8
ChainResidueDetails
ALYS26

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:19237750, ECO:0000269|Ref.7
ChainResidueDetails
AGLN83

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:19237750, ECO:0000269|PubMed:23485416, ECO:0000269|Ref.8
ChainResidueDetails
ASER112

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:19121323, ECO:0000269|PubMed:23485416, ECO:0000269|Ref.7, ECO:0007744|PDB:3SPT, ECO:0007744|PDB:4HCQ
ChainResidueDetails
AASP114

site_idSWS_FT_FI7
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:23485416, ECO:0000269|Ref.8
ChainResidueDetails
AARG344
ALYS362
ATYR377

site_idSWS_FT_FI8
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|Ref.7
ChainResidueDetails
AASN388
AALA391
ASER416

site_idSWS_FT_FI9
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631
ChainResidueDetails
AASN397

site_idSWS_FT_FI10
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|Ref.7
ChainResidueDetails
AALA434

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609
ChainResidueDetails
ATHR2

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup) => ECO:0000269|PubMed:20066036
ChainResidueDetails
ALYS362

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PDB entries from 2024-09-04

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