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4I9A

Crystal Structure of Sus scrofa Quinolinate Phosphoribosyltransferase in Complex with Nicotinate Mononucleotide

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004514molecular_functionnicotinate-nucleotide diphosphorylase (carboxylating) activity
A0005737cellular_componentcytoplasm
A0009435biological_processNAD biosynthetic process
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0019363biological_processpyridine nucleotide biosynthetic process
A0034213biological_processquinolinate catabolic process
A0042802molecular_functionidentical protein binding
B0000166molecular_functionnucleotide binding
B0004514molecular_functionnicotinate-nucleotide diphosphorylase (carboxylating) activity
B0005737cellular_componentcytoplasm
B0009435biological_processNAD biosynthetic process
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0019363biological_processpyridine nucleotide biosynthetic process
B0034213biological_processquinolinate catabolic process
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE NCN A 301
ChainResidue
AARG138
AGLY249
AGLY250
ASER268
ALEU269
AGLY270
ALYS139
AHIS160
AARG161
ALYS171
AGLU201
AASP222
AGLU246
ASER248

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE NCN B 301
ChainResidue
BARG138
BLYS139
BHIS160
BARG161
BLYS171
BGLU201
BASP222
BSER248
BGLY249
BLEU269
BGLY270

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q15274
ChainResidueDetails
AARG102
BARG102

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000305|PubMed:23626766, ECO:0007744|PDB:4I9A
ChainResidueDetails
AGLY270
BARG138
BHIS160
BLYS171
BGLU201
BASP222
BSER248
BGLY270
ALYS171
AGLU201
AASP222
ASER248
AARG138
AHIS160

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PDB entries from 2024-06-12

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