Research workbench
Formyl-CoA transferase in complex with oxalyl-CoA
Analyse Formyl-CoA transferase in complex with oxalyl-CoA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1T4C
- Type
- protein
- Length
- 854 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Formyl-coenzyme a transferase
- EC
- 2.8.3.16
- UniProt
- O06644
- Ligands
- COA
- Pockets
- 13 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Formyl-coenzyme a transferase (EC 2.8.3.16) | protein | 427 | 39% helix, 13% strand | O06644 |
| B | Formyl-coenzyme a transferase (EC 2.8.3.16) | protein | 427 | 38% helix, 14% strand | O06644 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 508 | 0.73 | 0.82 | 56 | COA |
| 2 | 62 | 0.72 | 0.98 | 34 | empty |
| 3 | 129 | 0.71 | 0.91 | 45 | empty |
| 4 | 323 | 0.67 | 0.82 | 42 | COA |
| 5 | 223 | 0.59 | 0.81 | 32 | empty |
Interfaces
1 interface between chains.
- A–B · 6368 Ų buried · 77 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent, 1 modified (covalent ligand, nonstandard).
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O06644
- Elsewhere: RCSB PDB 1T4C · PDBe 1T4C · UniProt O06644
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