Research workbench
Crystal structure of uncharacterized conserved protein from thermus thermophilus
Analyse Crystal structure of uncharacterized conserved protein from thermus thermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Z06
- Type
- protein
- Length
- 1,008 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative uncharacterized protein TTHA0625
- UniProt
- Q5SKL8
- Ligands
- CO
- Pockets
- 11 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Putative uncharacterized protein TTHA0625 | protein | 252 | 27% helix, 31% strand | Q5SKL8 |
Ligands and binding sites
- CO · Cobalt (II) ion · metal · 13 copies · chains A, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 714 | 0.74 | 0.80 | 89 | CO |
| 2 | 328 | 0.64 | 0.80 | 50 | empty |
| 3 | 327 | 0.63 | 0.79 | 42 | empty |
| 4 | 117 | 0.55 | 0.83 | 23 | empty |
| 5 | 130 | 0.51 | 0.81 | 29 | empty |
Interfaces
6 interfaces between chains.
- C–D · 1528 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 1518 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 453 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 443 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 367 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2Z06 · Crystal structure of uncharacterized conserved protein from Thermus thermophilus · 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 Q5SKL8
- Elsewhere: RCSB PDB 2Z06 · PDBe 2Z06 · UniProt Q5SKL8
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