Research workbench
Structure of the E. COLI puta proline dehydrogenase domain reduced by dithionite and complexed with proline
Analyse Structure of the E. COLI puta proline dehydrogenase domain reduced by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FZN
- Type
- protein
- Length
- 449 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional protein puta, proline dehydrogenase (ec 1.5.99.8) (proline oxidase)
- EC
- 1.5.99.8
- UniProt
- P09546
- Ligands
- FAD, PRO
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional protein puta, proline dehydrogenase (ec 1.5.99.8) (proline oxidase) (EC 1.5.99.8) | protein | 449 | 55% helix, 10% strand | P09546 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 466 | 0.84 | 0.91 | 41 | FAD, PRO |
| 2 | 166 | 0.51 | 0.78 | 23 | empty |
| 3 | 101 | 0.44 | 0.79 | 24 | empty |
| 4 | 56 | 0.31 | 0.76 | 13 | empty |
Compared structures
- 2FZN · Structure of the E. coli PutA proline dehydrogenase domain reduced by dithionite and… · the same entry in another collection · chain A against A, TM-score 1.00
- P09546 · AlphaFold monomer V2.0 prediction for bifunctional protein puta (P09546) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 P09546
- Elsewhere: RCSB PDB 2FZN · PDBe 2FZN · UniProt P09546
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