Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4XTW

Mycobacterium tuberculosis biotin ligase complexed with bisubstrate inhibitor 46 with azide in place of 2'OH

Functional Information from GO Data
ChainGOidnamespacecontents
A0004077molecular_functionbiotin-[acetyl-CoA-carboxylase] ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0008284biological_processpositive regulation of cell population proliferation
A0009374molecular_functionbiotin binding
A0016874molecular_functionligase activity
A0032991cellular_componentprotein-containing complex
A0036211biological_processprotein modification process
A0042803molecular_functionprotein homodimerization activity
B0004077molecular_functionbiotin-[acetyl-CoA-carboxylase] ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0008284biological_processpositive regulation of cell population proliferation
B0009374molecular_functionbiotin binding
B0016874molecular_functionligase activity
B0032991cellular_componentprotein-containing complex
B0036211biological_processprotein modification process
B0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues27
Detailsbinding site for residue 44M A 301
ChainResidue
ASER38
AGLY73
ATRP74
AALA75
AGLN81
AILE83
AASN130
ALYS138
AGLY141
AILE142
ALEU143
ATHR39
AVAL155
AASN158
AVAL166
AASP167
AALA170
AHOH435
AHOH452
AHOH456
AASN40
AGLN63
AGLY66
AARG67
AGLY68
AARG69
AARG72

site_idAC2
Number of Residues4
Detailsbinding site for residue EDO A 302
ChainResidue
AGLY99
AGLN243
AGLY244
ASER258

site_idAC3
Number of Residues27
Detailsbinding site for residue 44M B 300
ChainResidue
AHOH416
BSER38
BTHR39
BASN40
BGLN63
BGLY66
BARG67
BGLY68
BARG69
BARG72
BGLY73
BTRP74
BALA75
BGLN81
BILE83
BASN130
BLYS138
BGLY141
BILE142
BLEU143
BVAL155
BGLY156
BASN158
BVAL166
BASP167
BALA170
BHOH433

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:24723382
ChainResidueDetails
BARG67
BLYS138
ASER38
AGLN63
AARG67
ALYS138
BSER38
BGLN63

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon