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3C2O

Crystal structure of the quinolinate phosphoribosyl transferase (BNA6) from Sachharomyces cerevisiae complexed with quinolinate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004514molecular_functionnicotinate-nucleotide diphosphorylase (carboxylating) activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0009435biological_processNAD biosynthetic process
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0019363biological_processpyridine nucleotide biosynthetic process
A0034213biological_processquinolinate catabolic process
A0034354biological_process'de novo' NAD biosynthetic process from tryptophan
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NTM A 300
ChainResidue
AARG107
ATHR142
AARG143
AHIS165
AARG166
AMET174
ASER256
ASER276
AHOH322

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:18321072
ChainResidueDetails
AARG107
AARG166
ALYS176
AASP227

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ATHR142
ASER256

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLU206

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qpr
ChainResidueDetails
AGLU206
ALYS144
AASP227

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qpr
ChainResidueDetails
AARG107

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qpr
ChainResidueDetails
AGLU204
ALYS144
AASP227

site_idMCSA1
Number of Residues1
DetailsM-CSA 945
ChainResidueDetails
ALYS144electrostatic stabiliser

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PDB entries from 2024-07-10

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