Research workbench
C-myc DNA unwinding element binding protein
Analyse C-myc DNA unwinding element binding protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OKV
- Type
- protein
- Length
- 597 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable D-tyrosyl-TRNA(TYR) deacylase 1
- EC
- 3.1.-.-
- UniProt
- Q8TEA8
- Ligands
- MG
- Pockets
- 6 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D | Probable D-tyrosyl-TRNA(TYR) deacylase 1 (EC 3.1.-.-) | protein | 149 | 28% helix, 38% strand | Q8TEA8 |
| B | Probable D-tyrosyl-TRNA(TYR) deacylase 1 (EC 3.1.-.-) | protein | 150 | 27% helix, 41% strand | Q8TEA8 |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 623 | 0.73 | 0.80 | 71 | empty |
| 2 | 171 | 0.53 | 0.79 | 28 | empty |
| 3 | 147 | 0.51 | 0.79 | 25 | empty |
| 4 | 190 | 0.51 | 0.77 | 34 | empty |
| 5 | 138 | 0.49 | 0.79 | 29 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1699 Ų buried · 41 hydrogen bonds · protein-protein
- A–B · 1688 Ų buried · 41 hydrogen bonds · protein-protein
- B–C · 309 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 146 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 118 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
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 Q8TEA8
- Elsewhere: RCSB PDB 2OKV · PDBe 2OKV · UniProt Q8TEA8
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