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2YQJ

Crystal Structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida albicans, in the reaction-completed form

Functional Information from GO Data
ChainGOidnamespacecontents
A0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
A0005737cellular_componentcytoplasm
A0006048biological_processUDP-N-acetylglucosamine biosynthetic process
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0070569molecular_functionuridylyltransferase activity
B0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
B0005737cellular_componentcytoplasm
B0006048biological_processUDP-N-acetylglucosamine biosynthetic process
B0016740molecular_functiontransferase activity
B0016779molecular_functionnucleotidyltransferase activity
B0070569molecular_functionuridylyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1101
ChainResidue
AGLY114
ATHR115
AARG116
AUD11001

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1102
ChainResidue
AARG285
ALYS328
AARG332
AHOH1415

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 1201
ChainResidue
ATHR77
AHOH1445
AASN74

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 2102
ChainResidue
BLYS328
BARG332

site_idAC5
Number of Residues28
DetailsBINDING SITE FOR RESIDUE UD1 A 1001
ChainResidue
AMET109
AGLY111
AGLY112
AARG116
AMET168
AGLN199
APRO224
AGLY226
AASN227
ACYS255
AVAL256
AVAL293
AGLY294
AGLU309
ATYR310
AASN335
AVAL337
APHE393
APHE395
APHE417
ALYS421
ASO41101
AHOH1366
AHOH1386
AHOH1389
AHOH1402
AHOH1404
AHOH1439

site_idAC6
Number of Residues26
DetailsBINDING SITE FOR RESIDUE UD1 B 2001
ChainResidue
BMET109
BGLY111
BGLY112
BARG116
BMET168
BGLN199
BPRO224
BGLY226
BASN227
BCYS255
BVAL256
BASP257
BVAL293
BGLY294
BGLU309
BTYR310
BASN335
BVAL337
BPHE393
BPHE395
BPHE417
BLYS421
BHOH2114
BHOH2119
BHOH2171
BHOH2175

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1301
ChainResidue
APHE196
AASN237
AHOH1313
AHOH1377
BGLN6
BHOH2174

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9M9P3
ChainResidueDetails
AMET109
BGLY226
BASP257
BLYS389
ALYS123
AGLN199
AGLY226
AASP257
ALYS389
BMET109
BLYS123
BGLN199

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASN227
ALYS421
BASN227
BLYS421

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PDB entries from 2024-09-11

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