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4E1K

GlmU in complex with a Quinazoline Compound

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
A0008360biological_processregulation of cell shape
A0009245biological_processlipid A biosynthetic process
A0009252biological_processpeptidoglycan biosynthetic process
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0019134molecular_functionglucosamine-1-phosphate N-acetyltransferase activity
A0046872molecular_functionmetal ion binding
A0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
ATHR170
A0N5505
AHOH660

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AHOH788
AHOH969
AGLY14
ALYS15
AGLY16
ATHR17
ALYS25
AHOH644

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AARG331
AARG333
APRO334

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PG4 A 504
ChainResidue
AASN72
AASN386
AASP388
APHE402
ATHR420
AALA423

site_idAC5
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 0N5 A 505
ChainResidue
ALEU11
AALA12
AALA13
AGLY14
AVAL26
ATHR82
ATYR103
AASP105
AASN169
AVAL223
AGLU224
ASO4501
AHOH673
AHOH687
AHOH756
AHOH811

Functional Information from PROSITE/UniProt
site_idPS00101
Number of Residues29
DetailsHEXAPEP_TRANSFERASES Hexapeptide-repeat containing-transferases signature. VGsdTqLvapVkVAngAtIGagTtItrdV
ChainResidueDetails
AVAL403-VAL431

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01631
ChainResidueDetails
AHIS363

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:18029420, ECO:0000269|PubMed:22721802, ECO:0000269|PubMed:25262942
ChainResidueDetails
ALEU11
ATYR103

site_idSWS_FT_FI3
Number of Residues11
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631
ChainResidueDetails
ALYS25
AALA423
AARG440
AASP105
AASN227
AARG333
ALYS351
ATYR366
AASN377
AASN386
ASER405

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:25262942
ChainResidueDetails
AGLN76

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:18029420, ECO:0000269|PubMed:25262942
ChainResidueDetails
AGLY81

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:18029420
ChainResidueDetails
AGLY140
AGLU154
AASN169

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0ACC7, ECO:0000255|HAMAP-Rule:MF_01631
ChainResidueDetails
AALA380

222036

PDB entries from 2024-07-03

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