Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3DK5

Crystal Structure of Apo-GlmU from Mycobacterium tuberculosis

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 Residues4
DetailsBINDING SITE FOR RESIDUE MG A 496
ChainResidue
AASP417
AASP417
AASP417
AHOH530

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 497
ChainResidue
ASER392
ASER392
AASP417
AASP417
AASP417

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
AGLY88
AGLY151
AGLU166
AASN181
AASN239
ALEU12

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

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon