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4U0O

Crystal structure of Thermosynechococcus elongatus Lipoyl Synthase 2 complexed with MTA and DTT

Functional Information from GO Data
ChainGOidnamespacecontents
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0009107biological_processlipoate biosynthetic process
B0009249biological_processprotein lipoylation
B0016740molecular_functiontransferase activity
B0016992molecular_functionlipoate synthase activity
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 Residues5
Detailsbinding site for residue SF4 B 301
ChainResidue
BCYS63
BCYS67
BPHE69
BCYS70
BDTT303

site_idAC2
Number of Residues6
Detailsbinding site for residue SF4 B 302
ChainResidue
BTHR55
BSER283
BCYS37
BCYS42
BASN44
BCYS48

site_idAC3
Number of Residues7
Detailsbinding site for residue DTT B 303
ChainResidue
BILE36
BTHR104
BSER105
BSF4301
BMTA304
BHOH450
BHOH505

site_idAC4
Number of Residues12
Detailsbinding site for residue MTA B 304
ChainResidue
BPHE69
BASN169
BGLU171
BMET210
BGLN239
BLEU241
BARG281
BSER283
BDTT303
BHOH490
BHOH483
BHOH484

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00206, ECO:0000269|PubMed:25100160, ECO:0007744|PDB:4U0O, ECO:0007744|PDB:4U0P
ChainResidueDetails
BCYS37
BCYS42
BCYS48
BCYS63
BCYS67
BCYS70

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00206, ECO:0000269|PubMed:25100160, ECO:0007744|PDB:4U0O
ChainResidueDetails
BSER283

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PDB entries from 2024-09-18

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