MolNFT v1 · #125956 · protein
Structure of full length unliganded cody from bacillus subtilis
5LOJ · GTP-sensing transcriptional pleiotropic repressor cody: “Structure of full length unliganded cody from bacillus subtilis”. X-ray diffraction, 7 pockets (best druggability 0.73). MolNFT v1 #125956 on GenesisL1: 3D structure, binding…
- PDB
- 5LOJ
- Type
- protein
- Length
- 510 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTP-sensing transcriptional pleiotropic repressor cody
- UniProt
- P39779
- Pockets
- 7 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | GTP-sensing transcriptional pleiotropic repressor cody | protein | 255 | 45% helix, 14% strand | P39779 |
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 159 | 0.73 | 0.90 | 25 | empty |
| 2 | 501 | 0.73 | 0.82 | 61 | empty |
| 3 | 140 | 0.64 | 0.86 | 25 | empty |
| 4 | 57 | 0.57 | 0.89 | 24 | empty |
| 5 | 63 | 0.57 | 0.88 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 881 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 5LOJ · Structure of full length unliganded CodY from Bacillus subtilis · the same entry in another collection · chain A against A, TM-score 1.00
- P39779 · AlphaFold monomer V2.0 prediction for GTP-sensing transcriptional pleiotropic repressor… · a predicted model of the same protein · chain B against A, TM-score 0.89
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 P39779
- Elsewhere: RCSB PDB 5LOJ · PDBe 5LOJ · UniProt P39779
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