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5ONC

Catabolism of the Cholesterol Side Chain in Mycobacterium tuberculosis is Controlled by a Redox-Sensitive Thiol Switch

Functional Information from GO Data
ChainGOidnamespacecontents
A0003988molecular_functionacetyl-CoA C-acyltransferase activity
A0006635biological_processfatty acid beta-oxidation
A0006707biological_processcholesterol catabolic process
A0008203biological_processcholesterol metabolic process
A0010124biological_processphenylacetate catabolic process
A0016042biological_processlipid catabolic process
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0042802molecular_functionidentical protein binding
B0003988molecular_functionacetyl-CoA C-acyltransferase activity
B0006635biological_processfatty acid beta-oxidation
B0006707biological_processcholesterol catabolic process
B0008203biological_processcholesterol metabolic process
B0010124biological_processphenylacetate catabolic process
B0016042biological_processlipid catabolic process
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue CL A 401
ChainResidue
ACYS118
ASER354

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 402
ChainResidue
AARG212
APHE215
AARG216

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 403
ChainResidue
AASN315
ACYS377

site_idAC4
Number of Residues3
Detailsbinding site for residue CL A 404
ChainResidue
ASER124
AHIS25
AALA26

site_idAC5
Number of Residues1
Detailsbinding site for residue CL B 401
ChainResidue
BSER354

Functional Information from PROSITE/UniProt
site_idPS00737
Number of Residues17
DetailsTHIOLASE_2 Thiolases signature 2. NvnGGaIAlGHPvGcTG
ChainResidueDetails
AASN337-GLY353

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-thioester intermediate => ECO:0000305|PubMed:25482540, ECO:0007744|PDB:4UBV
ChainResidueDetails
ACYS93
BCYS93

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:25482540, ECO:0007744|PDB:4UBV
ChainResidueDetails
AHIS347
BHIS347

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:25482540
ChainResidueDetails
ACYS377
BCYS377

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:25482540, ECO:0007744|PDB:4UBT
ChainResidueDetails
BGLN151
BGLY379
AGLN151
AGLY379

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:25482540, ECO:0007744|PDB:4UBT, ECO:0007744|PDB:4UBV
ChainResidueDetails
AARG221
BARG221

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:25482540, ECO:0007744|PDB:4UBT, ECO:0007744|PDB:4UBU, ECO:0007744|PDB:4UBV
ChainResidueDetails
ASER246
BSER246

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PDB entries from 2024-06-12

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