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3TWD

glmuC1 in complex with an antibacterial inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
A0006048biological_processUDP-N-acetylglucosamine biosynthetic process
A0016740molecular_functiontransferase activity
A0019134molecular_functionglucosamine-1-phosphate N-acetyltransferase activity
B0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
B0006048biological_processUDP-N-acetylglucosamine biosynthetic process
B0016740molecular_functiontransferase activity
B0019134molecular_functionglucosamine-1-phosphate N-acetyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B 1
ChainResidue
BHOH4
BHOH158
BHOH183
BARG333
BLYS351
BHIS363
BTYR366
BASN386
BLYS392

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 2
ChainResidue
AHOH12
AHOH104
AHOH142
AARG333
ALYS351
AHIS363
ATYR366
AASN386
ALYS392

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE GOB A 1
ChainResidue
AHOH114
AHOH205
AASN377
AGLY379
AALA380
ACYS385
ATYR387
AASP388
APHE402
AGLY404
ASER405
AVAL410
AALA411
AALA422
AALA423
AARG440
APRO452
AHOH472

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GOB B 454
ChainResidue
BHOH116
BHOH220
BASN377
BGLY379
BALA380
BCYS385
BASN386
BTYR387
BASP388
BPHE402
BGLY404
BSER405
BVAL410
BALA411
BALA422
BALA423
BARG440
BTRP449
BPRO452
BHOH455
BHOH472

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01631
ChainResidueDetails
AHIS363
BHIS363

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:11329257, ECO:0000269|PubMed:17473010
ChainResidueDetails
AARG333
ALYS351
ATYR366
BARG333
BLYS351
BTYR366

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:11329257, ECO:0000269|PubMed:17473010, ECO:0000269|PubMed:21984832
ChainResidueDetails
AASN377
ASER405
AALA423
AARG440
BASN377
BSER405
BALA423
BARG440

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:17473010, ECO:0000269|PubMed:21984832
ChainResidueDetails
AALA380
BALA380

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631
ChainResidueDetails
AASN386
BASN386

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 811
ChainResidueDetails

site_idMCSA2
Number of Residues
DetailsM-CSA 811
ChainResidueDetails

237992

PDB entries from 2025-06-25

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