Research workbench
Crystal structure of the unswapped form of P19A/L28Q/N67D bs-RNase
Analyse Crystal structure of the unswapped form of P19A/L28Q/N67D bs-RNase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BCM
- Type
- protein
- Length
- 238 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Seminal ribonuclease
- EC
- 3.1.27.5
- UniProt
- P00669
- Ligands
- PO4
- Pockets
- 3 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Seminal ribonuclease (EC 3.1.27.5) | protein | 119 | 22% helix, 37% strand | P00669 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 178 | 0.45 | 0.75 | 18 | empty |
| 2 | 119 | 0.36 | 0.73 | 19 | empty |
| 3 | 52 | 0.24 | 0.72 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 371 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 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 P00669
- Elsewhere: RCSB PDB 3BCM · PDBe 3BCM · UniProt P00669
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