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5KTT

Crystal structure of Pyrococcus horikoshii quinolinate synthase (NadA) with bound L-malate and Fe4S4 cluster

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
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
A0046872molecular_functionmetal ion binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue SF4 A 401
ChainResidue
ACYS83
AMET85
ACYS170
AGLU198
ACYS256
ALMR402

site_idAC2
Number of Residues12
Detailsbinding site for residue LMR A 402
ChainResidue
AMET61
ATYR109
AASN111
AHIS196
AGLU198
ASER212
ATHR213
ASF4401
AHOH507
AHIS21
ATYR23
AASP37

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000269|PubMed:31390192, ECO:0000305|PubMed:15937336, ECO:0000305|PubMed:27224840, ECO:0000305|PubMed:27404889
ChainResidueDetails
AHIS21
ASER38
ATYR109

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000269|PubMed:27224840, ECO:0000269|PubMed:27404889, ECO:0000269|PubMed:31390192, ECO:0007744|PDB:4ZK6, ECO:0007744|PDB:5KTM, ECO:0007744|PDB:5KTN, ECO:0007744|PDB:5KTO, ECO:0007744|PDB:5KTP, ECO:0007744|PDB:5KTR, ECO:0007744|PDB:5KTS, ECO:0007744|PDB:5KTT
ChainResidueDetails
ACYS83
ACYS170
ACYS256

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000269|PubMed:31390192, ECO:0000305|PubMed:15937336, ECO:0000305|PubMed:27404889
ChainResidueDetails
ASER126
AHIS196
ATHR213

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PDB entries from 2024-07-10

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