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4P3X

Structure of the Fe4S4 quinolinate synthase NadA from Thermotoga maritima

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
A0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue SF4 A 301
ChainResidue
ACYS81
AASN109
ACYS168
AVAL170
ACYS254
AHOH533
AHOH535
AHOH552

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 302
ChainResidue
AHIS-4
AHIS-1
AHIS0
AHOH404
AMET-6

site_idAC3
Number of Residues7
Detailsbinding site for residue MPD A 303
ChainResidue
AASP57
AGLU61
AARG77
AGLU218
AVAL276
AHOH417
AHOH420

site_idAC4
Number of Residues7
Detailsbinding site for residue MPD A 304
ChainResidue
AHIS-5
APRO169
AVAL170
AGLN172
AMET251
AHOH442
AHOH478

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
AHIS19
ASER36
ASER124
AHIS193
ATHR210

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
ACYS81
ACYS168
ACYS254

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

222036

PDB entries from 2024-07-03

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