Research workbench
Pandda analysis group deposition -- AAR2/RNASEH in complex with fragment F2X-entry A07, dmso-free
Analyse Pandda analysis group deposition -- AAR2/RNASEH in complex with fragment… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5R08
- Type
- protein
- Length
- 537 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P33334, P32357
- Ligands
- R8A
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 237 | — | P33334 |
| B | — | protein | 300 | — | P32357 |
Ligands and binding sites
- R8A · (2-aminopyridin-3-yl)methanol · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5R08 · PanDDA analysis group deposition -- Aar2/RNaseH in complex with fragment F2X-Entry A07… · the same entry in another collection · chain A against A, TM-score 1.00
- P32357 · AlphaFold monomer V2.0 prediction for A1 cistron-splicing factor AAR2 (P32357) · a predicted model of the same protein · chain B against A, 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 P33334
- Every structure of UniProt P32357
- Elsewhere: RCSB PDB 5R08 · PDBe 5R08 · UniProt P33334 · UniProt P32357
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