MolNFT v1 · #88465 · protein
Crystal structure of the N-terminal colied-coil domain of human DNA excision repair protein ercc-6
4CVO: “Crystal structure of the N-terminal colied-coil domain of human DNA excision repair protein ercc-6”. X-ray diffraction, 1 ligand (MG). MolNFT v1 #88465 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4CVO
- Type
- protein
- Length
- 69 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA excision repair protein ercc-6
- EC
- 3.6.4.-
- UniProt
- Q03468
- Ligands
- MG
Structure
x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA excision repair protein ercc-6 (EC 3.6.4.-) | protein | 69 | 78% helix, 0% strand | Q03468 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4CVO · Crystal structure of the N-terminal colied-coil domain of human DNA excision repair… · the same entry in another collection · chain A against A, TM-score 1.00
- Q03468 · AlphaFold monomer V2.0 prediction for DNA excision repair protein ercc-6 (Q03468) · a predicted model of the same protein · chain A against A, TM-score 0.70
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 Q03468
- Elsewhere: RCSB PDB 4CVO · PDBe 4CVO · UniProt Q03468
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