Research workbench
Crystal structure of ribonuclease SA2 with guanosine-2'-cyclophosphate
Analyse Crystal structure of ribonuclease SA2 with guanosine-2'-cyclophosphate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DGY
- Type
- protein
- Length
- 277 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease
- EC
- 3.1.4.8
- UniProt
- Q53752
- Ligands
- 2GP, BGC, SO4
- Pockets
- 4 · best druggability 0.64
Structure
x-ray diffraction · 3 distinct chains · 16% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease (EC 3.1.4.8) | protein | 92 | 16% helix, 26% strand | Q53752 |
| B | Ribonuclease (EC 3.1.4.8) | protein | 94 | 16% helix, 22% strand | Q53752 |
| C | Ribonuclease (EC 3.1.4.8) | protein | 91 | 15% helix, 26% strand | Q53752 |
Ligands and binding sites
- 2GP · Guanosine-2'-monophosphate · ligand · chains B
- BGC · beta-D-glucopyranose · sugar · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 201 | 0.64 | 0.84 | 35 | empty |
| 2 | 77 | 0.51 | 0.85 | 17 | empty |
| 3 | 139 | 0.44 | 0.76 | 25 | SO4 |
| 4 | 57 | 0.28 | 0.74 | 22 | empty |
Interfaces
2 interfaces between chains.
- B–C · 887 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 532 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 3DGY · Crystal structure of ribonuclease Sa2 with guanosine-2'-cyclophosphate · the same entry in another collection · chain B against B, 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 Q53752
- Elsewhere: RCSB PDB 3DGY · PDBe 3DGY · UniProt Q53752
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