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Structure of the E. COLI puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid
Analyse Structure of the E. COLI puta proline dehydrogenase domain (residues 86-630)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MWV
- Type
- protein
- Length
- 499 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional protein puta
- EC
- 1.5.5.2, 1.2.1.88
- UniProt
- A0A383H020
- Ligands
- FAD, ZPJ
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 60% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional protein puta (EC 1.5.5.2, 1.2.1.88) | protein | 499 | 60% helix, 9% strand | A0A383H020 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- ZPJ · cyclopropanecarboxylic acid · ligand · chains A
- PG4 · Tetraethylene glycol · additive · chains A
- 1PE · Pentaethylene glycol · additive · 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 | 41 | FAD, ZPJ |
| 2 | 156 | 0.51 | 0.79 | 24 | empty |
| 3 | 68 | 0.33 | 0.75 | 17 | empty |
| 4 | 52 | 0.30 | 0.76 | 10 | empty |
Compared structures
- 7MWV · Structure of the E. coli PutA proline dehydrogenase domain (residues 86-630) complexed… · the same entry in another collection · 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 A0A383H020
- Elsewhere: RCSB PDB 7MWV · PDBe 7MWV · UniProt A0A383H020
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