Research workbench
Crystal structure of the central domain of human ERCC1
Analyse Crystal structure of the central domain of human ERCC1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A1I
- Type
- protein
- Length
- 129 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA excision repair protein ercc-1
- UniProt
- P07992
- Ligands
- HG
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA excision repair protein ercc-1 | protein | 129 | 42% helix, 22% strand | P07992 |
Ligands and binding sites
- HG · Mercury (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 66 | 0.33 | 0.76 | 14 | empty |
Compared structures
- 2A1I · Crystal Structure of the Central Domain of Human ERCC1 · the same entry in another collection · chain A against A, TM-score 1.00
- P07992 · AlphaFold monomer V2.0 prediction for DNA excision repair protein ercc-1 (P07992) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P07992
- Elsewhere: RCSB PDB 2A1I · PDBe 2A1I · UniProt P07992
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