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Structure of KU80 von willebrand domain S229A mutant complexed with xlf ku binding motif
Analyse Structure of KU80 von willebrand domain S229A mutant complexed with xlf ku… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TYX
- Type
- protein
- Length
- 439 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- X-ray repair cross-complementing protein 5; Lys-gly-leu-phe-met
- EC
- 3.6.4.-
- UniProt
- A0A1L8EVE5
- Pockets
- 4 · best druggability 0.45
Structure
x-ray diffraction · 4 distinct chains · 44% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | X-ray repair cross-complementing protein 5 (EC 3.6.4.-) | protein | 211 | 45% helix, 19% strand | A0A1L8EVE5 |
| B | X-ray repair cross-complementing protein 5 (EC 3.6.4.-) | protein | 216 | 43% helix, 19% strand | A0A1L8EVE5 |
| C | Lys-gly-leu-phe-met | protein | 5 | 60% helix, 0% strand | — |
| D | Lys-gly-leu-phe-met | protein | 7 | 43% helix, 0% strand | — |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 76 | 0.45 | 0.81 | 25 | empty |
| 2 | 67 | 0.39 | 0.79 | 17 | empty |
| 3 | 94 | 0.39 | 0.76 | 25 | empty |
| 4 | 71 | 0.32 | 0.75 | 13 | empty |
Interfaces
3 interfaces between chains.
- A–C · 381 Ų buried · 2 hydrogen bonds · protein-protein
- B–D · 357 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 152 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6TYX · Structure of Ku80 von Willebrand domain S229A mutant complexed with XLF Ku Binding Motif · 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 A0A1L8EVE5
- Elsewhere: RCSB PDB 6TYX · PDBe 6TYX · UniProt A0A1L8EVE5
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