Research workbench
Crystal structure of hmces cross-linked to DNA abasic site
Analyse Crystal structure of hmces cross-linked to DNA abasic site in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OE7
- Type
- protein + DNA
- Length
- 273 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q96FZ2
- Ligands
- UNX
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 258 | — | Q96FZ2 |
| C | — | dna | 6 | — | — |
| B | — | dna | 9 | — | — |
Ligands and binding sites
- UNX · Unknown atom or ion · ion · 4 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6OE7 · Crystal structure of HMCES cross-linked to DNA abasic site · the same entry in another collection · chain B against B, TM-score 1.00
- Q96FZ2 · AlphaFold monomer V2.0 prediction for abasic site processing protein hmces (Q96FZ2) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q96FZ2
- Elsewhere: RCSB PDB 6OE7 · PDBe 6OE7 · UniProt Q96FZ2
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