Research workbench
Crystal structure of the tudor domain of human ERCC6-L2
Analyse Crystal structure of the tudor domain of human ERCC6-L2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HQ9
- Type
- protein
- Length
- 118 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA excision repair protein ercc-6-like 2
- EC
- 3.6.4.-
- UniProt
- Q5T890
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA excision repair protein ercc-6-like 2 (EC 3.6.4.-) | protein | 60 | 5% helix, 48% strand | Q5T890 |
| B | DNA excision repair protein ercc-6-like 2 (EC 3.6.4.-) | protein | 58 | 5% helix, 52% strand | Q5T890 |
Interfaces
1 interface between chains.
- A–B · 399 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 6HQ9 · Crystal structure of the Tudor domain of human ERCC6-L2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q5T890 · AlphaFold monomer V2.0 prediction for DNA excision repair protein ercc-6-like 2 (Q5T890) · a predicted model of the same protein · chain A against A, TM-score 0.90
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 Q5T890
- Elsewhere: RCSB PDB 6HQ9 · PDBe 6HQ9 · UniProt Q5T890
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