Research workbench
Crystal structure of TT1027 from thermus thermophilus HB8
Analyse Crystal structure of TT1027 from thermus thermophilus HB8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UFR
- Type
- protein
- Length
- 666 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pyr mRNA-binding attenuation protein
- UniProt
- P83822
- Ligands
- CL
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Pyr mRNA-binding attenuation protein | protein | 167 | 31% helix, 37% strand | P83822 |
| C, D | Pyr mRNA-binding attenuation protein | protein | 166 | 30% helix, 37% strand | P83822 |
Ligands and binding sites
- CL · Chloride ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 508 | 0.75 | 0.83 | 56 | empty |
| 2 | 87 | 0.37 | 0.76 | 18 | CL |
| 3 | 82 | 0.35 | 0.75 | 21 | CL |
| 4 | 95 | 0.34 | 0.74 | 20 | CL |
| 5 | 81 | 0.34 | 0.75 | 19 | CL |
Interfaces
4 interfaces between chains.
- C–D · 845 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 820 Ų buried · 13 hydrogen bonds · protein-protein
- B–D · 819 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 814 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 1UFR · Crystal Structure of TT1027 from Thermus thermophilus HB8 · the same entry in another collection · chain C against C, 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 P83822
- Elsewhere: RCSB PDB 1UFR · PDBe 1UFR · UniProt P83822
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