Research workbench
Determination and restrained least-squares refinement of the crystal structures of ribonuclease sa and its complex with 3'-guanylic acid at 1.8 ångströms resolution
Analyse Determination and restrained least-squares refinement of the crystal structures… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2SAR
- Type
- protein
- Length
- 192 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease sa
- EC
- 3.1.4.8
- UniProt
- P05798
- Ligands
- 3GP, SO4
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ribonuclease sa (EC 3.1.4.8) | protein | 96 | 15% helix, 27% strand | P05798 |
Ligands and binding sites
- 3GP · Guanosine-3'-monophosphate · ligand · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 141 | 0.53 | 0.81 | 27 | empty |
| 2 | 115 | 0.42 | 0.77 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 243 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2SAR · Determination and restrained least-squares refinement of the crystal structures of… · the same entry in another collection · chain A against A, TM-score 1.00
- P05798 · AlphaFold monomer V2.0 prediction for guanyl-specific ribonuclease sa (P05798) · 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 P05798
- Elsewhere: RCSB PDB 2SAR · PDBe 2SAR · UniProt P05798
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