Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6G74

Structure of the Y21F variant of quinolinate synthase in complex with phthalate

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008987molecular_functionquinolinate synthetase A activity
A0009435biological_processNAD+ biosynthetic process
A0016740molecular_functiontransferase activity
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
A0019363biological_processpyridine nucleotide biosynthetic process
A0019805biological_processquinolinate biosynthetic process
A0034628biological_process'de novo' NAD+ biosynthetic process from L-aspartate
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008987molecular_functionquinolinate synthetase A activity
B0009435biological_processNAD+ biosynthetic process
B0016740molecular_functiontransferase activity
B0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
B0019363biological_processpyridine nucleotide biosynthetic process
B0019805biological_processquinolinate biosynthetic process
B0034628biological_process'de novo' NAD+ biosynthetic process from L-aspartate
B0046872molecular_functionmetal ion binding
B0051536molecular_functioniron-sulfur cluster binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue SF4 A 301
ChainResidue
ACYS81
AASN109
ACYS168
AGLU195
ACYS254
APHT302
AHOH580

site_idAC2
Number of Residues14
Detailsbinding site for residue PHT A 302
ChainResidue
AASP35
ASER36
AASN109
ASER124
AHIS193
AGLU195
ATHR210
ASF4301
AHOH404
AHOH554
AHOH566
AHOH580
AHIS19
APHE21

site_idAC3
Number of Residues7
Detailsbinding site for residue SF4 B 301
ChainResidue
BCYS81
BASN109
BCYS168
BVAL170
BCYS254
BPHT302
BHOH575

site_idAC4
Number of Residues15
Detailsbinding site for residue PHT B 302
ChainResidue
BHIS19
BPHE21
BASP35
BSER36
BASN109
BSER124
BHIS193
BGLU195
BTHR210
BSF4301
BHOH408
BHOH519
BHOH541
BHOH571
BHOH575

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00568","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27545412","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"29641168","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"30855610","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00568","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24650327","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27545412","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29641168","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4P3X","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5F33","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5F35","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5F3D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LQM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LQS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00568","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27545412","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"29641168","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon