MolNFT v1 · #51577 · protein + DNA
Molecular basis of human xpc gene recognition and cleavage by engineered homing endonuclease heterodimers
2VBL: “Molecular basis of human xpc gene recognition and cleavage by engineered homing endonuclease heterodimers”. X-ray diffraction. MolNFT v1 #51577 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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
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