7O4V
Structure of Mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with oxidized nicotinamide adenine dinucleotide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003857 | molecular_function | (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity |
| A | 0004300 | molecular_function | enoyl-CoA hydratase activity |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016509 | molecular_function | long-chain (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0070403 | molecular_function | NAD+ binding |
| B | 0003857 | molecular_function | (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity |
| B | 0004300 | molecular_function | enoyl-CoA hydratase activity |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006635 | biological_process | fatty acid beta-oxidation |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016509 | molecular_function | long-chain (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0070403 | molecular_function | NAD+ binding |
| C | 0003985 | molecular_function | acetyl-CoA C-acetyltransferase activity |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0016746 | molecular_function | acyltransferase activity |
| C | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| D | 0003985 | molecular_function | acetyl-CoA C-acetyltransferase activity |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0016746 | molecular_function | acyltransferase activity |
| D | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue NAD B 801 |
| Chain | Residue |
| B | ALA333 |
| B | GLU414 |
| B | LEU418 |
| B | LYS419 |
| B | VAL422 |
| B | ASN439 |
| B | SER441 |
| B | HIS462 |
| B | GLY334 |
| B | MET335 |
| B | MET336 |
| B | ASP355 |
| B | VAL356 |
| B | ALA411 |
| B | VAL412 |
| B | PHE413 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 802 |
| Chain | Residue |
| B | PRO259 |
| B | GLY293 |
| B | GLN294 |
| B | VAL295 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 803 |
| Chain | Residue |
| B | HIS-7 |
| B | HIS-6 |
| B | HIS-8 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 804 |
| Chain | Residue |
| B | SER658 |
| B | THR659 |
| B | ALA660 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 805 |
| Chain | Residue |
| B | GLY25 |
| B | SER26 |
| B | THR27 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 D 501 |
| Chain | Residue |
| D | THR317 |
| D | ARG382 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 D 502 |
| Chain | Residue |
| A | VAL274 |
| A | ASP275 |
| D | HIS24 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 D 503 |
| Chain | Residue |
| D | ASN380 |
| D | ARG382 |
| D | ARG402 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 D 504 |
| Chain | Residue |
| D | SER163 |
| D | ARG164 |
| D | ASN249 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 D 505 |
| Chain | Residue |
| B | PRO631 |
| B | LEU632 |
| D | HIS243 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 D 506 |
| Chain | Residue |
| D | ARG195 |
| D | LEU201 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 D 507 |
| Chain | Residue |
| D | PRO193 |
| D | ARG195 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 D 508 |
| Chain | Residue |
| D | LYS177 |
| D | ASP345 |
| D | GLU346 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 C 501 |
| Chain | Residue |
| C | ARG382 |
| C | ARG382 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 C 502 |
| Chain | Residue |
| C | ARG382 |
| C | ARG383 |
| C | ARG402 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 C 503 |
| Chain | Residue |
| B | GLN273 |
| B | VAL274 |
| B | ASP275 |
| C | HIS24 |
| site_id | AD8 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 C 504 |
| Chain | Residue |
| C | PRO193 |
| C | ARG195 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 C 505 |
| Chain | Residue |
| C | SER163 |
| C | ARG164 |
| C | ASN249 |
| site_id | AE1 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 C 506 |
| Chain | Residue |
| C | ARG195 |
| C | LEU201 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 C 507 |
| Chain | Residue |
| C | LYS177 |
| C | ASP345 |
| C | GLU346 |
| site_id | AE3 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 C 508 |
| Chain | Residue |
| C | THR317 |
| C | VAL318 |
| site_id | AE4 |
| Number of Residues | 16 |
| Details | binding site for residue NAD A 801 |
| Chain | Residue |
| A | ALA333 |
| A | GLY334 |
| A | MET335 |
| A | MET336 |
| A | ASP355 |
| A | VAL356 |
| A | ALA411 |
| A | VAL412 |
| A | GLU414 |
| A | LEU418 |
| A | LYS419 |
| A | VAL422 |
| A | ASN439 |
| A | THR440 |
| A | SER441 |
| A | HIS462 |
| site_id | AE5 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 802 |
| Chain | Residue |
| A | PRO259 |
| A | GLY293 |
| A | GLN294 |
| A | VAL295 |
| site_id | AE6 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 803 |
| Chain | Residue |
| A | PRO631 |
| A | LEU632 |
| C | HIS243 |
| site_id | AE7 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 804 |
| Chain | Residue |
| A | ARG702 |
| A | LEU719 |
| A | SER720 |
| site_id | AE8 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 805 |
| Chain | Residue |
| A | ARG598 |
| A | ARG612 |
| site_id | AE9 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 806 |
| Chain | Residue |
| A | HIS-8 |
| A | HIS-6 |
| A | HIS-9 |
| A | HIS-7 |
Functional Information from PROSITE/UniProt
| site_id | PS00098 |
| Number of Residues | 19 |
| Details | THIOLASE_1 Thiolases acyl-enzyme intermediate signature. LNRfCASGLeAVntaaqkV |
| Chain | Residue | Details |
| D | LEU88-VAL106 |
| site_id | PS00099 |
| Number of Residues | 14 |
| Details | THIOLASE_3 Thiolases active site. ALITLCIGgGmGvA |
| Chain | Residue | Details |
| D | ALA384-ALA397 |
| site_id | PS00737 |
| Number of Residues | 17 |
| Details | THIOLASE_2 Thiolases signature 2. NvnGGaIAmGHPlGaTG |
| Chain | Residue | Details |
| D | ASN349-GLY365 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Acyl-thioester intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10020","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)","evidences":[{"source":"PubMed","id":"20066036","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
