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

7O4S

Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme with Coenzyme A bound at the hydratase, thiolase active sites and additional binding site (CoA(ECH2))

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003857molecular_function3-hydroxyacyl-CoA dehydrogenase activity
A0004300molecular_functionenoyl-CoA hydratase activity
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006631biological_processfatty acid metabolic process
A0006635biological_processfatty acid beta-oxidation
A0009056biological_processcatabolic process
A0009274cellular_componentpeptidoglycan-based cell wall
A0016042biological_processlipid catabolic process
A0016491molecular_functionoxidoreductase activity
A0016509molecular_functionlong-chain-3-hydroxyacyl-CoA dehydrogenase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0016829molecular_functionlyase activity
A0070403molecular_functionNAD+ binding
B0000166molecular_functionnucleotide binding
B0003857molecular_function3-hydroxyacyl-CoA dehydrogenase activity
B0004300molecular_functionenoyl-CoA hydratase activity
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006631biological_processfatty acid metabolic process
B0006635biological_processfatty acid beta-oxidation
B0009056biological_processcatabolic process
B0009274cellular_componentpeptidoglycan-based cell wall
B0016042biological_processlipid catabolic process
B0016491molecular_functionoxidoreductase activity
B0016509molecular_functionlong-chain-3-hydroxyacyl-CoA dehydrogenase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0016829molecular_functionlyase activity
B0070403molecular_functionNAD+ binding
C0005886cellular_componentplasma membrane
C0009274cellular_componentpeptidoglycan-based cell wall
C0016746molecular_functionacyltransferase activity
C0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
D0005886cellular_componentplasma membrane
D0009274cellular_componentpeptidoglycan-based cell wall
D0016746molecular_functionacyltransferase activity
D0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue SO4 A 801
ChainResidue
AGLY293
AGLN294
AVAL295

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 802
ChainResidue
AVAL274
AASP275
CHIS24

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 803
ChainResidue
AHIS-8
AHIS-6
AHIS-7

site_idAC4
Number of Residues2
Detailsbinding site for residue SO4 A 804
ChainResidue
AARG598
AARG612

site_idAC5
Number of Residues3
Detailsbinding site for residue SO4 A 805
ChainResidue
APRO631
ALEU632
DHIS243

site_idAC6
Number of Residues3
Detailsbinding site for residue SO4 A 806
ChainResidue
ATHR657
ASER658
ATHR659

site_idAC7
Number of Residues2
Detailsbinding site for residue GOL A 807
ChainResidue
AASP710
AARG711

site_idAC8
Number of Residues14
Detailsbinding site for residue COA A 808
ChainResidue
ATHR27
AALA66
AGLY68
AASP69
AVAL70
ALYS71
ALEU114
AGLY115
AGLY116
APRO140
AGLU141
ALEU144
AARG175
AGLN308

site_idAC9
Number of Residues7
Detailsbinding site for residue COA A 809
ChainResidue
APHE160
AASN164
ASER168
AVAL169
ALYS180
AGLU183
AILE184

site_idAD1
Number of Residues2
Detailsbinding site for residue GOL A 810
ChainResidue
AMET30
APHE287

site_idAD2
Number of Residues3
Detailsbinding site for residue SO4 B 801
ChainResidue
BGLY293
BGLN294
BVAL295

site_idAD3
Number of Residues3
Detailsbinding site for residue SO4 B 802
ChainResidue
BVAL274
BASP275
DHIS24

site_idAD4
Number of Residues2
Detailsbinding site for residue SO4 B 803
ChainResidue
BLEU632
CHIS243

site_idAD5
Number of Residues5
Detailsbinding site for residue SO4 B 804
ChainResidue
BTHR657
BSER658
BTHR659
BALA660
BHOH903

site_idAD6
Number of Residues2
Detailsbinding site for residue SO4 B 805
ChainResidue
BPRO220
BLYS223

site_idAD7
Number of Residues2
Detailsbinding site for residue GOL B 806
ChainResidue
AHIS-6
BALA12

site_idAD8
Number of Residues12
Detailsbinding site for residue COA B 807
ChainResidue
BTHR27
BVAL29
BALA66
BGLY68
BASP69
BVAL70
BLYS71
BLEU114
BGLY116
BGLU141
BARG175
BPHE304

site_idAD9
Number of Residues7
Detailsbinding site for residue COA B 808
ChainResidue
BPHE160
BASN164
BSER168
BVAL169
BLYS180
BGLU183
BILE184

site_idAE1
Number of Residues3
Detailsbinding site for residue GOL B 809
ChainResidue
BGLY68
BMET73
BILE91

site_idAE2
Number of Residues2
Detailsbinding site for residue SO4 B 810
ChainResidue
BHIS-8
BHIS-7

site_idAE3
Number of Residues3
Detailsbinding site for residue SO4 C 501
ChainResidue
CTHR317
CASP319
CARG382

site_idAE4
Number of Residues3
Detailsbinding site for residue SO4 C 502
ChainResidue
CSER163
CARG164
CASN249

site_idAE5
Number of Residues1
Detailsbinding site for residue SO4 C 503
ChainResidue
CARG195

site_idAE6
Number of Residues2
Detailsbinding site for residue SO4 C 504
ChainResidue
CPRO193
CARG195

site_idAE7
Number of Residues4
Detailsbinding site for residue SO4 C 505
ChainResidue
CHIS43
CPRO44
CASP45
CLEU46

site_idAE8
Number of Residues4
Detailsbinding site for residue SO4 C 506
ChainResidue
CGLU346
CARG173
CLYS177
CASP345

site_idAE9
Number of Residues2
Detailsbinding site for residue SO4 C 507
ChainResidue
CARG382
CARG402

site_idAF1
Number of Residues13
Detailsbinding site for residue COA C 508
ChainResidue
CMET127
CGLN149
CARG210
CTHR213
CLEU218
CLEU221
CPHE225
CGLY254
CGLY255
CSER258
CPHE330
CHIS359
CLEU361

site_idAF2
Number of Residues2
Detailsbinding site for residue PAP C 509
ChainResidue
BGLN629
CTRP244

site_idAF3
Number of Residues2
Detailsbinding site for residue SO4 C 510
ChainResidue
CTYR186
CARG378

site_idAF4
Number of Residues3
Detailsbinding site for residue SO4 D 501
ChainResidue
DARG382
DARG383
DARG402

site_idAF5
Number of Residues3
Detailsbinding site for residue SO4 D 502
ChainResidue
DARG195
DLEU201
DHOH608

site_idAF6
Number of Residues2
Detailsbinding site for residue SO4 D 503
ChainResidue
DPRO193
DARG195

site_idAF7
Number of Residues3
Detailsbinding site for residue SO4 D 504
ChainResidue
DSER163
DARG164
DASN249

site_idAF8
Number of Residues5
Detailsbinding site for residue SO4 D 505
ChainResidue
DHIS43
DPRO44
DASP45
DLEU46
DGLN278

site_idAF9
Number of Residues2
Detailsbinding site for residue SO4 D 506
ChainResidue
DARG382
DARG382

site_idAG1
Number of Residues13
Detailsbinding site for residue COA D 507
ChainResidue
DLYS19
DGLN149
DGLN175
DARG210
DTHR213
DLEU218
DLEU221
DPHE225
DGLY254
DGLY255
DSER258
DILE260
DLEU361

site_idAG2
Number of Residues2
Detailsbinding site for residue ADP D 508
ChainResidue
AGLN629
DTRP244

Functional Information from PROSITE/UniProt
site_idPS00098
Number of Residues19
DetailsTHIOLASE_1 Thiolases acyl-enzyme intermediate signature. LNRfCASGLeAVntaaqkV
ChainResidueDetails
CLEU88-VAL106

site_idPS00099
Number of Residues14
DetailsTHIOLASE_3 Thiolases active site. ALITLCIGgGmGvA
ChainResidueDetails
CALA384-ALA397

site_idPS00737
Number of Residues17
DetailsTHIOLASE_2 Thiolases signature 2. NvnGGaIAmGHPlGaTG
ChainResidueDetails
CASN349-GLY365

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-thioester intermediate => ECO:0000250
ChainResidueDetails
CCYS92
DCYS92

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10020
ChainResidueDetails
CHIS359
CCYS389
DHIS359
DCYS389

site_idSWS_FT_FI3
Number of Residues4
DetailsCROSSLNK: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup) => ECO:0000269|PubMed:20066036
ChainResidueDetails
CLYS189
DLYS189

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon