Research workbench
Structure of a vertebrate RNA binding domain of telomerase (trbd)
Analyse Structure of a vertebrate RNA binding domain of telomerase (trbd) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LMO
- Type
- protein
- Length
- 1,004 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Telomerase reverse transcriptase
- UniProt
- Q4KTA7
- Pockets
- 15 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 59% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Telomerase reverse transcriptase | protein | 251 | 59% helix, 5% strand | Q4KTA7 |
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 979 | 0.87 | 0.88 | 79 | empty |
| 2 | 797 | 0.87 | 0.90 | 71 | empty |
| 3 | 1123 | 0.79 | 0.80 | 92 | empty |
| 4 | 194 | 0.65 | 0.85 | 35 | empty |
| 5 | 307 | 0.63 | 0.80 | 41 | empty |
Interfaces
4 interfaces between chains.
- A–D · 3089 Ų buried · 26 hydrogen bonds · protein-protein
- B–C · 2891 Ų buried · 25 hydrogen bonds · protein-protein
- B–D · 496 Ų buried · 1 hydrogen bond · protein-protein
- A–B · 113 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 4LMO · Structure of a vertebrate RNA binding domain of telomerase (TRBD) · the same entry in another collection · chain A against A, TM-score 1.00
- Q4KTA7 · AlphaFold monomer V2.0 prediction for telomerase reverse transcriptase (Q4KTA7) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 Q4KTA7
- Elsewhere: RCSB PDB 4LMO · PDBe 4LMO · UniProt Q4KTA7
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