Research workbench
Human RNase H catalytic domain mutant D210N in complex with 14-mer RNA/DNA hybrid
Analyse Human RNase H catalytic domain mutant D210N in complex with 14-mer RNA/DNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QKK
- Type
- protein + DNA + RNA
- Length
- 1,805 residues
- Chains
- 23
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O60930
Structure
x-ray diffraction · 13 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, G, K, O, T | — | rna | 14 | — | — |
| D, H, L, P, U | — | dna | 14 | — | — |
| X | — | rna | 13 | — | — |
| Z | — | dna | 11 | — | — |
| A | — | protein | 154 | — | O60930 |
| B, J | — | protein | 151 | — | O60930 |
| E | — | protein | 149 | — | O60930 |
| F | — | protein | 152 | — | O60930 |
| I | — | protein | 149 | — | O60930 |
| M | — | protein | 145 | — | O60930 |
| N | — | protein | 146 | — | O60930 |
| R, S | — | protein | 148 | — | O60930 |
| W | — | protein | 148 | — | O60930 |
Compared structures
- 2QKK · Human RNase H catalytic domain mutant D210N in complex with 14-mer RNA/DNA hybrid · the same entry in another collection · chain X against X, TM-score 1.00
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 O60930
- Elsewhere: RCSB PDB 2QKK · PDBe 2QKK · UniProt O60930
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