MolNFT v1 · #20826 · protein + DNA
Structural mechanisms of camptothecin resistance by mutations in human topoisomerase I
1RR8: “Structural mechanisms of camptothecin resistance by mutations in human topoisomerase I”. X-ray diffraction. MolNFT v1 #20826 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1RR8
- Type
- protein + DNA
- Length
- 538 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P11387
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | dna | 22 | — | — |
| B | — | dna | 22 | — | — |
| C | — | protein | 494 | — | P11387 |
Compared structures
- 1RR8 · Structural Mechanisms of Camptothecin Resistance by Mutations in Human Topoisomerase I · the same entry in another collection · chain A against A, TM-score 1.00
- P11387 · AlphaFold monomer V2.0 prediction for DNA topoisomerase 1 (P11387) · a predicted model of the same protein · chain C 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 P11387
- Elsewhere: RCSB PDB 1RR8 · PDBe 1RR8 · UniProt P11387
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