Research workbench
X-ray structure of mouse ribonuclease inhibitor complexed with mouse ribonuclease 1
Analyse X-ray structure of mouse ribonuclease inhibitor complexed with mouse… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TSR
- Type
- protein
- Length
- 2,305 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease pancreatic; Ribonuclease inhibitor
- EC
- 3.1.27.5
- UniProt
- P00683, Q91VI7
- Pockets
- 20 · best druggability 0.76
Structure
x-ray diffraction · 5 distinct chains · 32% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease pancreatic (EC 3.1.27.5) | protein | 124 | 21% helix, 35% strand | P00683 |
| B | Ribonuclease pancreatic (EC 3.1.27.5) | protein | 123 | 21% helix, 36% strand | P00683 |
| C | Ribonuclease pancreatic (EC 3.1.27.5) | protein | 117 | 21% helix, 32% strand | P00683 |
| D | Ribonuclease pancreatic (EC 3.1.27.5) | protein | 113 | 23% helix, 34% strand | P00683 |
| E, F, G, H | Ribonuclease inhibitor | protein | 457 | 43% helix, 13% strand | Q91VI7 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 13 copies · chains A, E, F, B, G, C, H, D
- PEG · Di(hydroxyethyl)ether · additive · chains E, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1068 | 0.76 | 0.79 | 106 | empty |
| 2 | 636 | 0.72 | 0.80 | 53 | empty |
| 3 | 698 | 0.72 | 0.79 | 63 | empty |
| 4 | 664 | 0.71 | 0.79 | 59 | empty |
| 5 | 327 | 0.69 | 0.83 | 54 | empty |
Interfaces
7 interfaces between chains.
- E–G · 2141 Ų buried · 35 hydrogen bonds · protein-protein
- F–H · 2081 Ų buried · 34 hydrogen bonds · protein-protein
- C–G · 1508 Ų buried · 21 hydrogen bonds · protein-protein
- D–H · 1489 Ų buried · 20 hydrogen bonds · protein-protein
- B–F · 1401 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 disulfide (disulfide).
Compared structures
- 3TSR · X-ray structure of mouse ribonuclease inhibitor complexed with mouse ribonuclease 1 · the same entry in another collection · chain H against H, TM-score 1.00
- P00683 · AlphaFold monomer V2.0 prediction for ribonuclease pancreatic (P00683) · a predicted model of the same protein · chain C against A, TM-score 0.99
- Q91VI7 · AlphaFold monomer V2.0 prediction for ribonuclease inhibitor (Q91VI7) · a predicted model of the same protein · chain E against A, TM-score 0.98
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 P00683
- Every structure of UniProt Q91VI7
- Elsewhere: RCSB PDB 3TSR · PDBe 3TSR · UniProt P00683 · UniProt Q91VI7
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