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4G3P

Crystal structure of GlmU from Mycobacterium tuberculosis Snapshot 3

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0000902biological_processcell morphogenesis
A0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
A0005737cellular_componentcytoplasm
A0006048biological_processUDP-N-acetylglucosamine biosynthetic process
A0009252biological_processpeptidoglycan biosynthetic process
A0019134molecular_functionglucosamine-1-phosphate N-acetyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE POP A 501
ChainResidue
AGLY17
AHOH791
AHOH798
ATHR18
AARG19
AMG504
AUD1506
AHOH633
AHOH755
AHOH756
AHOH757

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
AASP417
AASP417
AASP417
AHOH759
AHOH759
AHOH759

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 503
ChainResidue
AASP114
AASN239
AUD1506
AHOH753
AHOH754

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 504
ChainResidue
AGLN205
APOP501
AHOH755
AHOH756
AHOH798

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CO A 505
ChainResidue
AASP417
AASP417
AASP417

site_idAC6
Number of Residues30
DetailsBINDING SITE FOR RESIDUE UD1 A 506
ChainResidue
ALEU12
AALA13
AALA14
AGLY15
AARG19
ALYS26
AGLN83
APRO86
ALEU87
AGLY88
ATHR89
AALA92
AGLY113
AASP114
ATYR150
AGLY151
AGLU166
AASN181
ATYR209
ATHR211
AASN239
APOP501
ACO503
AHOH642
AHOH658
AHOH717
AHOH754
AHOH755
AHOH791
AHOH794

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
AGLY151
AGLU166
AASN181
AASN239
ALEU12
AGLY88

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
ALYS362
ATYR377
AARG344

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 2024-06-12

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