Research workbench
Molecular basis of human xpc gene recognition and cleavage by engineered homing endonuclease heterodimers
Analyse Molecular basis of human xpc gene recognition and cleavage by engineered homing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VBL
- Type
- protein + DNA
- Length
- 352 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P05725
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 152 | — | P05725 |
| B | — | protein | 152 | — | P05725 |
| C | — | dna | 14 | — | — |
| E | — | dna | 14 | — | — |
| S | — | dna | 10 | — | — |
| T | — | dna | 10 | — | — |
Compared structures
- 2VBL · Molecular basis of human XPC gene recognition and cleavage by engineered homing… · the same entry in another collection · chain C against C, TM-score 1.00
- P05725 · AlphaFold monomer V2.0 prediction for DNA endonuclease I-crei (P05725) · 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 P05725
- Elsewhere: RCSB PDB 2VBL · PDBe 2VBL · UniProt P05725
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.