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6I0K

Structure of quinolinate synthase in complex with 4-mercaptophthalic acid

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 aspartate
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue SF4 A 301
ChainResidue
ACYS81
AASN109
ACYS168
ACYS254
AGZ8302

site_idAC2
Number of Residues14
Detailsbinding site for residue GZ8 A 302
ChainResidue
AMET59
AASN109
ASER124
AHIS193
ASER209
ATHR210
ASF4301
AHOH413
AHOH494
AHOH506
AHIS19
APHE21
AASP35
ASER36

site_idAC3
Number of Residues5
Detailsbinding site for residue PO4 A 303
ChainResidue
AHIS-1
AHIS0
AMET1
AVAL2
AHOH544

site_idAC4
Number of Residues3
Detailsbinding site for residue CL A 304
ChainResidue
AASN67
AASP69
AHOH571

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000305|PubMed:27545412, ECO:0000305|PubMed:29641168, ECO:0000305|PubMed:30855610
ChainResidueDetails
AHIS193
ATHR210
AHIS19
ASER36
ASER124

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000269|PubMed:24650327, ECO:0000269|PubMed:27545412, ECO:0000269|PubMed:29641168, ECO:0007744|PDB:4P3X, ECO:0007744|PDB:5F33, ECO:0007744|PDB:5F35, ECO:0007744|PDB:5F3D, ECO:0007744|PDB:5LQM, ECO:0007744|PDB:5LQS
ChainResidueDetails
ACYS168
ACYS254
ACYS81

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000305|PubMed:27545412, ECO:0000305|PubMed:29641168
ChainResidueDetails
ATYR107

218500

PDB entries from 2024-04-17

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