MolNFT v1 · #171089 · protein
Magnesium chelatase H subunit (chlh) E660D variant from synechocystis SP.PCC6803
6YT0 · Mg-chelatase subunit chlh: “Magnesium chelatase H subunit (chlh) E660D variant from synechocystis SP.PCC6803”. X-ray diffraction, 20 pockets (best druggability 0.85). MolNFT v1 #171089 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6YT0
- Type
- protein
- Length
- 2,455 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mg-chelatase subunit chlh
- UniProt
- P73020
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Mg-chelatase subunit chlh | protein | 1207 | 50% helix, 14% strand | P73020 |
| A | Mg-chelatase subunit chlh | protein | 1248 | 50% helix, 14% strand | P73020 |
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 353 | 0.85 | 0.94 | 51 | empty |
| 2 | 276 | 0.83 | 0.94 | 37 | empty |
| 3 | 188 | 0.83 | 0.97 | 39 | empty |
| 4 | 956 | 0.78 | 0.80 | 75 | empty |
| 5 | 51 | 0.71 | 0.98 | 18 | empty |
Interfaces
1 interface between chains.
- B–A · 645 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 6YT0 · Magnesium chelatase H subunit (ChlH) E660D variant from Synechocystis sp.PCC6803 · the same entry in another collection · chain B against B, 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 P73020
- Elsewhere: RCSB PDB 6YT0 · PDBe 6YT0 · UniProt P73020
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.