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

4KNX

Hin GlmU Bound to WG176

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 Residues14
DetailsBINDING SITE FOR RESIDUE 1S9 A 501
ChainResidue
ALEU11
AASN169
ATHR170
AVAL223
AGLY225
AHOH922
AALA12
AALA13
AGLY14
AGLN76
AGLN79
ATHR82
ATYR103
AASP105

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PG4 A 502
ChainResidue
AASN72
AASN386
AASP388
APHE402
ATHR420
AALA423
AHOH645
AHOH900
AHOH1126

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PG4 A 503
ChainResidue
AASP157
AASN159
AGLN162
AASN189
AASN191
AALA192
AGLY194
AHOH878
AHOH1133
AHOH1155

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 504
ChainResidue
AASP406
AASP406
AASP406
AHOH623
AHOH623
AHOH623

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 505
ChainResidue
AASP406
AASP406
AASP406
AHOH629
AHOH629
AHOH629

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 506
ChainResidue
AGLY14
ALYS15
AGLY16
ATHR17
ALYS25
AHOH908
AHOH1151

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 507
ChainResidue
AARG331
AARG333
APRO334
AHOH1092

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 508
ChainResidue
ALYS360
AASN362
AHIS363
AHOH1096
AHOH1098
AHOH1099

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 509
ChainResidue
AHIS57
AGLY58
AHOH801
AHOH1065

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

220113

PDB entries from 2024-05-22

PDB statisticsPDBj update infoContact PDBjnumon