Research workbench
Arsh of paracoccus denitrificans
Analyse Arsh of paracoccus denitrificans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PLE
- Type
- protein
- Length
- 892 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NADPH-dependent FMN reductase
- UniProt
- A1B6S0
- Pockets
- 8 · best druggability 0.84
Structure
x-ray diffraction · 4 distinct chains · 36% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADPH-dependent FMN reductase | protein | 222 | 36% helix, 16% strand | A1B6S0 |
| B | NADPH-dependent FMN reductase | protein | 227 | 35% helix, 15% strand | A1B6S0 |
| C | NADPH-dependent FMN reductase | protein | 223 | 37% helix, 15% strand | A1B6S0 |
| D | NADPH-dependent FMN reductase | protein | 220 | 37% helix, 16% strand | A1B6S0 |
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 231 | 0.84 | 0.97 | 25 | empty |
| 2 | 434 | 0.63 | 0.77 | 54 | empty |
| 3 | 409 | 0.63 | 0.77 | 54 | empty |
| 4 | 267 | 0.61 | 0.79 | 35 | empty |
| 5 | 358 | 0.58 | 0.76 | 43 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2323 Ų buried · 22 hydrogen bonds · protein-protein
- A–B · 2241 Ų buried · 18 hydrogen bonds · protein-protein
- B–D · 1308 Ų buried · 20 hydrogen bonds · protein-protein
- A–C · 1294 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 260 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 7PLE · ArsH of Paracoccus denitrificans · 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 A1B6S0
- Elsewhere: RCSB PDB 7PLE · PDBe 7PLE · UniProt A1B6S0
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