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4KNR

Hin GlmU bound to WG188

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 Residues13
DetailsBINDING SITE FOR RESIDUE 1S8 A 501
ChainResidue
ALEU11
AVAL223
AHOH937
AHOH1017
AHOH1018
AALA12
AALA13
AGLY14
ATHR82
ATYR103
AASP105
AASN169
ATHR170

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PG4 A 502
ChainResidue
AASN72
ATYR387
AASP388
AGLY422
AALA423
AILE438
AHOH998
AHOH999
AHOH1000

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PG4 A 503
ChainResidue
AASP157
AASN159
AGLN162
AASN189
AASN190
AASN191
AALA192
AGLN193
AGLY194
AHOH968

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 504
ChainResidue
AASP406
AASP406
AASP406
AHOH605
AHOH605
AHOH605

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 505
ChainResidue
AASP406
AASP406
AASP406
AHOH994
AHOH994
AHOH994

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 506
ChainResidue
ALYS15
AGLY16
ATHR17
ALYS25
AHOH815
AHOH877

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 507
ChainResidue
AARG333
APRO334
AHOH790

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 508
ChainResidue
ALYS360
AASN362
AHIS363
AHOH624
AHOH823
AHOH993

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 509
ChainResidue
AHIS57
AGLY58
AHOH730

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 510
ChainResidue
AARG18
AASN227
AGLN231

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
AASN377
AASN386
ASER405
AALA423
AARG440
ALYS25
AASP105
AASN227
AARG333
ALYS351
ATYR366

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
AASN169
AGLY140
AGLU154

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

219869

PDB entries from 2024-05-15

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