MolNFT v1 · #182568 · protein
Structure of the E. COLI puta proline dehydrogenase domain (residues 86-630) complexed with 1,1-cyclobutanedicarboxylate
7MWT · Bifunctional protein puta: “Structure of the E. COLI puta proline dehydrogenase domain (residues 86-630) complexed with…”. X-ray diffraction, 3 ligands (FAD, ZPS, SO4), 5 pockets (best druggability 0.84). MolNFT v1 #182568 on…
- PDB
- 7MWT
- 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, ZPS, SO4
- Pockets
- 5 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 59% 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 | 59% helix, 9% strand | A0A383H020 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- ZPS · cyclobutane-1,1-dicarboxylic acid · ligand · chains A
- SO4 · Sulfate ion · ion · chains A
- PGE · Triethylene glycol · additive · chains A
- PG4 · Tetraethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 462 | 0.84 | 0.91 | 42 | FAD, ZPS |
| 2 | 125 | 0.47 | 0.79 | 20 | empty |
| 3 | 91 | 0.37 | 0.76 | 22 | empty |
| 4 | 67 | 0.35 | 0.77 | 18 | empty |
| 5 | 55 | 0.29 | 0.74 | 12 | empty |
Compared structures
- 7MWT · 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 7MWT · PDBe 7MWT · UniProt A0A383H020
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