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1FWY

CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE BOUND TO UDP-GLCNAC

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
A0009252biological_processpeptidoglycan biosynthetic process
A0019134molecular_functionglucosamine-1-phosphate N-acetyltransferase activity
B0000287molecular_functionmagnesium ion binding
B0000902biological_processcell morphogenesis
B0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
B0005737cellular_componentcytoplasm
B0006048biological_processUDP-N-acetylglucosamine biosynthetic process
B0009252biological_processpeptidoglycan biosynthetic process
B0019134molecular_functionglucosamine-1-phosphate N-acetyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 951
ChainResidue
AARG144
AGLY147
ALYS148
AVAL149
AVAL213
AALA214

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 A 952
ChainResidue
AGLN231

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 953
ChainResidue
BVAL213
BALA214
BARG144
BGLY147

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 954
ChainResidue
BASN227
BGLN231
BHOH638

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE UD1 A 501
ChainResidue
ALEU11
AALA13
AGLY14
AGLN76
AGLN79
ALEU80
AGLY81
ATHR82
ATYR103
AASP105
ATYR139
AGLY140
AGLU154
AASN169
ATYR197
AILE198
ATHR199
AHOH607

site_idAC6
Number of Residues18
DetailsBINDING SITE FOR RESIDUE UD1 B 502
ChainResidue
BLEU11
BALA13
BGLY14
BGLN76
BGLN79
BLEU80
BGLY81
BTHR82
BTYR103
BASP105
BTYR139
BGLY140
BGLU154
BASN169
BTYR197
BTHR199
BHOH594
BHOH603

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 901
ChainResidue
ATYR139
AVAL223
AGLU224
AHOH524

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 902
ChainResidue
BTYR139
BTHR170
BVAL223
BHOH563

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsRegion: {"description":"Linker","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10428949","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8555230","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10428949","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11329257","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17473010","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17473010","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2OI5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hv9
ChainResidueDetails
AARG18

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hv9
ChainResidueDetails
BARG18

site_idMCSA1
Number of Residues1
DetailsM-CSA 811
ChainResidueDetails
AARG18electrostatic stabiliser

site_idMCSA2
Number of Residues1
DetailsM-CSA 811
ChainResidueDetails
BARG18electrostatic stabiliser

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PDB entries from 2025-12-24

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