Research workbench
Structure of the HSDDB1-hscsa complex
Analyse Structure of the HSDDB1-hscsa complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4A11
- Type
- protein
- Length
- 1,456 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA damage-binding protein 1; DNA excision repair protein ercc-8
- UniProt
- Q16531, Q13216
- Pockets
- 17 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA damage-binding protein 1 | protein | 1091 | 5% helix, 54% strand | Q16531 |
| B | DNA excision repair protein ercc-8 | protein | 365 | 6% helix, 41% strand | Q13216 |
Pockets
17 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1077 | 0.86 | 0.87 | 129 | empty |
| 2 | 490 | 0.81 | 0.88 | 50 | empty |
| 3 | 539 | 0.75 | 0.82 | 43 | empty |
| 4 | 691 | 0.74 | 0.80 | 55 | empty |
| 5 | 319 | 0.67 | 0.82 | 47 | empty |
Interfaces
1 interface between chains.
- A–B · 2258 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 4A11 · Structure of the hsDDB1-hsCSA complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q13216 · AlphaFold monomer V2.0 prediction for DNA excision repair protein ercc-8 (Q13216) · a predicted model of the same protein · chain B against A, TM-score 1.00
- Q16531 · AlphaFold monomer V2.0 prediction for DNA damage-binding protein 1 (Q16531) · a predicted model of the same protein · chain A against A, TM-score 0.77
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 Q16531
- Every structure of UniProt Q13216
- Elsewhere: RCSB PDB 4A11 · PDBe 4A11 · UniProt Q16531 · UniProt Q13216
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