Research workbench
Crystal structure of TTHA0988 in space group P212121
Analyse Crystal structure of TTHA0988 in space group P212121 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OPF
- Type
- protein
- Length
- 1,471 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative uncharacterized protein TTHA0988
- UniProt
- Q5SJM0
- Ligands
- SO4
- Pockets
- 14 · best druggability 0.75
Structure
x-ray diffraction · 3 distinct chains · 15% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative uncharacterized protein TTHA0988 | protein | 490 | 15% helix, 36% strand | Q5SJM0 |
| B | Putative uncharacterized protein TTHA0988 | protein | 493 | 15% helix, 35% strand | Q5SJM0 |
| C | Putative uncharacterized protein TTHA0988 | protein | 488 | 15% helix, 36% strand | Q5SJM0 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B, C
- GOL · Glycerol · additive · 4 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 936 | 0.75 | 0.78 | 74 | empty |
| 2 | 947 | 0.75 | 0.78 | 71 | empty |
| 3 | 635 | 0.74 | 0.80 | 65 | empty |
| 4 | 332 | 0.68 | 0.82 | 42 | empty |
| 5 | 232 | 0.67 | 0.84 | 33 | empty |
Interfaces
2 interfaces between chains.
- B–C · 590 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 458 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 3OPF · Crystal structure of TTHA0988 in space group P212121 · 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 Q5SJM0
- Elsewhere: RCSB PDB 3OPF · PDBe 3OPF · UniProt Q5SJM0
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