Research workbench
Crystal structure of E. COLI puta proline dehydrogenase domain (residues 86-669) co-crystallized with L-lactate
Analyse Crystal structure of E. COLI puta proline dehydrogenase domain (residues… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TJ0
- Type
- protein
- Length
- 469 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional puta protein
- EC
- 1.5.99.8
- UniProt
- P09546
- Ligands
- FAD, 2OP
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional puta protein (EC 1.5.99.8) | protein | 469 | 57% helix, 10% strand | P09546 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- 2OP · (2S)-2-hydroxypropanoic acid · ligand · chains A
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 | 447 | 0.84 | 0.91 | 42 | FAD, 2OP |
| 2 | 161 | 0.53 | 0.79 | 26 | empty |
| 3 | 132 | 0.47 | 0.78 | 26 | empty |
| 4 | 84 | 0.35 | 0.75 | 16 | empty |
Compared structures
- 1TJ0 · Crystal structure of E. coli PutA proline dehydrogenase domain (residues 86-669)… · 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 0.88
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 1TJ0 · PDBe 1TJ0 · UniProt P09546
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