Research workbench
Crystal structure of pfl from E.COLI in complex with substrate analogue oxamate
Analyse Crystal structure of pfl from E.COLI in complex with substrate analogue oxamate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PFL
- Type
- protein
- Length
- 1,518 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (formate acetyltransferase 1)
- EC
- 2.3.1.54
- UniProt
- P09373
- Ligands
- OXM
- Pockets
- 11 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein (formate acetyltransferase 1) (EC 2.3.1.54) | protein | 759 | 47% helix, 12% strand | P09373 |
Ligands and binding sites
- OXM · Oxamic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 783 | 0.87 | 0.90 | 72 | empty |
| 2 | 94 | 0.75 | 0.97 | 29 | empty |
| 3 | 105 | 0.73 | 0.95 | 29 | empty |
| 4 | 60 | 0.68 | 0.95 | 24 | empty |
| 5 | 89 | 0.42 | 0.78 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 2058 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
- 3PFL · Crystal structure of pfl from E.COLI in complex with substrate analogue oxamate · the same entry in another collection · chain A against A, TM-score 1.00
- P09373 · AlphaFold monomer V2.0 prediction for formate acetyltransferase 1 (P09373) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 P09373
- Elsewhere: RCSB PDB 3PFL · PDBe 3PFL · UniProt P09373
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