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2YQS

Crystal structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida albicans, in the product-binding 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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1101
ChainResidue
AGLY114
ATHR115
AARG116
ALYS123
AHOH1425

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 1201
ChainResidue
AASN74
ATHR77

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE UD1 A 1001
ChainResidue
AGLY112
AARG116
AMET168
AGLN199
APRO224
AGLY226
AASN227
ACYS255
AVAL256
AVAL293
AGLY294
AGLU309
ATYR310
AASN335
AVAL337
APHE393
APHE395
ALYS421
AHOH1310
AHOH1394
AHOH1396
AHOH1478
AMET109
AGLY111

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1302
ChainResidue
AGLN7
AILE10
ALYS14
ATYR25

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1303
ChainResidue
ATHR92
ALEU96
ATYR467
AGLY468
AGLU470
AHOH1412

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9M9P3
ChainResidueDetails
AASP257
ALYS389
AMET109
ALYS123
AGLN199
AGLY226

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS421
AASN227

218500

PDB entries from 2024-04-17

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