Research workbench
RNase PO1 complexed with 3'GMP
Analyse RNase PO1 complexed with 3'GMP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WR2
- Type
- protein
- Length
- 606 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanyl-specific ribonuclease PO1
- EC
- 4.6.1.24
- UniProt
- P81762
- Ligands
- 3GP
- Pockets
- 8 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Guanyl-specific ribonuclease PO1 (EC 4.6.1.24) | protein | 101 | 12% helix, 33% strand | P81762 |
Ligands and binding sites
- 3GP · Guanosine-3'-monophosphate · ligand · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 265 | 0.62 | 0.80 | 36 | empty |
| 2 | 204 | 0.60 | 0.81 | 34 | empty |
| 3 | 258 | 0.51 | 0.74 | 32 | 3GP |
| 4 | 163 | 0.45 | 0.75 | 26 | 3GP |
| 5 | 81 | 0.35 | 0.75 | 14 | 3GP |
Interfaces
8 interfaces between chains.
- A–F · 328 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 312 Ų buried · 0 hydrogen bonds · protein-protein
- E–F · 311 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 290 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 267 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 disulfide (disulfide).
Compared structures
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 P81762
- Elsewhere: RCSB PDB 3WR2 · PDBe 3WR2 · UniProt P81762
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