Research workbench
Protelomerase tela R255A mutant complexed with DNA hairpin product
Analyse Protelomerase tela R255A mutant complexed with DNA hairpin product in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4E0J
- Type
- protein + DNA
- Length
- 351 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protelomerase; DNA (5'-D(*CP*AP*TP*AP*AP*TP*AP*AP*CP*AP*AP*TP*A)-3'); DNA (5'…
- UniProt
- Q7CWV1
- Ligands
- NA, CL
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · 3 distinct chains · 56% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protelomerase | protein | 319 | 56% helix, 7% strand | Q7CWV1 |
| C | DNA (5'-D(*CP*AP*TP*AP*AP*TP*AP*AP*CP*AP*AP*TP*A)-3') | dna | 13 | — | — |
| D | DNA (5'- D(*TP*CP*AP*TP*GP*AP*TP*AP*TP*TP*GP*TP*TP*AP*TP*TP*AP*TP*G)-3') | dna | 19 | — | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 438 | 0.74 | 0.84 | 38 | empty |
| 2 | 320 | 0.69 | 0.83 | 45 | NA |
Interfaces
3 interfaces between chains.
- A–D · 1767 Ų buried · 34 hydrogen bonds · protein-nucleic
- A–C · 977 Ų buried · 20 hydrogen bonds · protein-nucleic
- C–D · 680 Ų buried · 50 hydrogen bonds · nucleic-nucleic
Compared structures
- 4E0J · Protelomerase tela R255A mutant complexed with DNA hairpin product · 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 Q7CWV1
- Elsewhere: RCSB PDB 4E0J · PDBe 4E0J · UniProt Q7CWV1
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