5ONC
Catabolism of the Cholesterol Side Chain in Mycobacterium tuberculosis is Controlled by a Redox-Sensitive Thiol Switch
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003988 | molecular_function | acetyl-CoA C-acyltransferase activity |
A | 0006635 | biological_process | fatty acid beta-oxidation |
A | 0006707 | biological_process | cholesterol catabolic process |
A | 0008203 | biological_process | cholesterol metabolic process |
A | 0010124 | biological_process | phenylacetate catabolic process |
A | 0016042 | biological_process | lipid catabolic process |
A | 0016746 | molecular_function | acyltransferase activity |
A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
A | 0042802 | molecular_function | identical protein binding |
B | 0003988 | molecular_function | acetyl-CoA C-acyltransferase activity |
B | 0006635 | biological_process | fatty acid beta-oxidation |
B | 0006707 | biological_process | cholesterol catabolic process |
B | 0008203 | biological_process | cholesterol metabolic process |
B | 0010124 | biological_process | phenylacetate catabolic process |
B | 0016042 | biological_process | lipid catabolic process |
B | 0016746 | molecular_function | acyltransferase activity |
B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
B | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | binding site for residue CL A 401 |
Chain | Residue |
A | CYS118 |
A | SER354 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue CL A 402 |
Chain | Residue |
A | ARG212 |
A | PHE215 |
A | ARG216 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue CL A 403 |
Chain | Residue |
A | ASN315 |
A | CYS377 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue CL A 404 |
Chain | Residue |
A | SER124 |
A | HIS25 |
A | ALA26 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue CL B 401 |
Chain | Residue |
B | SER354 |
Functional Information from PROSITE/UniProt
site_id | PS00737 |
Number of Residues | 17 |
Details | THIOLASE_2 Thiolases signature 2. NvnGGaIAlGHPvGcTG |
Chain | Residue | Details |
A | ASN337-GLY353 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Acyl-thioester intermediate => ECO:0000305|PubMed:25482540, ECO:0007744|PDB:4UBV |
Chain | Residue | Details |
A | CYS93 | |
B | CYS93 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:25482540, ECO:0007744|PDB:4UBV |
Chain | Residue | Details |
A | HIS347 | |
B | HIS347 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:25482540 |
Chain | Residue | Details |
A | CYS377 | |
B | CYS377 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25482540, ECO:0007744|PDB:4UBT |
Chain | Residue | Details |
A | GLN151 | |
A | GLY379 | |
B | GLN151 | |
B | GLY379 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25482540, ECO:0007744|PDB:4UBT, ECO:0007744|PDB:4UBV |
Chain | Residue | Details |
A | ARG221 | |
B | ARG221 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25482540, ECO:0007744|PDB:4UBT, ECO:0007744|PDB:4UBU, ECO:0007744|PDB:4UBV |
Chain | Residue | Details |
A | SER246 | |
B | SER246 |