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5EXJ

Crystal structure of M. tuberculosis lipoyl synthase at 1.64 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0009107biological_processlipoate biosynthetic process
A0016740molecular_functiontransferase activity
A0016992molecular_functionlipoate synthase activity
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 Residues6
Detailsbinding site for residue SF4 A 401
ChainResidue
ACYS81
ACYS85
ACYS88
AARG192
APHE195
ADTV403

site_idAC2
Number of Residues9
Detailsbinding site for residue SF4 A 402
ChainResidue
AILE63
ACYS66
ATHR73
AARG290
ASER292
ATYR293
ACYS55
ACYS60
AASN62

site_idAC3
Number of Residues10
Detailsbinding site for residue DTV A 403
ChainResidue
AILE90
ATHR121
AGLY122
ALEU155
ASF4401
AHOH516
AHOH548
AHOH565
AHOH635
AHOH660

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00206, ECO:0000269|PubMed:27506792, ECO:0007744|PDB:5EXI, ECO:0007744|PDB:5EXJ
ChainResidueDetails
ACYS55
ACYS60
ACYS66
ASER292

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00206, ECO:0000269|PubMed:27506792, ECO:0007744|PDB:5EXI, ECO:0007744|PDB:5EXJ, ECO:0007744|PDB:5EXK
ChainResidueDetails
ACYS81
ACYS85
ACYS88

227111

PDB entries from 2024-11-06

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