MolNFT v1 · #162327 · protein
New max effector from magnaporthe oryzae
6R5J · Uncharacterized protein: “New max effector from magnaporthe oryzae”. X-ray diffraction, 1 pocket (best druggability 0.36). MolNFT v1 #162327 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6R5J
- Type
- protein
- Length
- 135 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- L7J9X7
- Pockets
- 1 · best druggability 0.36
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 67 | 0% helix, 57% strand | L7J9X7 |
| C | Uncharacterized protein | protein | 68 | 0% helix, 56% strand | L7J9X7 |
Ligands and binding sites
- P6G · Hexaethylene glycol · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 96 | 0.36 | 0.75 | 33 | empty |
Interfaces
1 interface between chains.
- A–C · 555 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 6R5J · New MAX Effector from Magnaporthe oryzae · 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 L7J9X7
- Elsewhere: RCSB PDB 6R5J · PDBe 6R5J · UniProt L7J9X7
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