MolNFT v2 · #132936 · protein
PanDDA analysis group deposition -- Auto-refined data of Aar2/RNaseH for ground state model 42, DMSO-free
5R1S: “PanDDA analysis group deposition -- Auto-refined data of Aar2/RNaseH for ground state model 42, DMSO-free”. X-ray diffraction at 2.05. MolNFT v2 #132936 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5R1S
- Type
- protein
- Length
- 537 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.05
- Source
- Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
- UniProt
- P33334, P32357
Structure
x-ray diffraction · resolution 2.05 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 237 | — | P33334 |
| B | — | protein | 300 | — | P32357 |
Compared structures
- 5R1S · Pandda analysis group deposition -- auto-refined data of AAR2/RNASEH for ground state… · 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
- P33334 · AlphaFold monomer V2.0 prediction for pre-mRNA-splicing factor 8 (P33334) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 5R1S · PDBe 5R1S · UniProt P33334 · UniProt P32357
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