MolNFT v1 · #110226 · protein
Crystal structure of sso-SMAP2
4XQ3 · Like-sm ribonucleoprotein core: “Crystal structure of sso-SMAP2”. X-ray diffraction, 3 pockets (best druggability 0.43). MolNFT v1 #110226 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4XQ3
- Type
- protein
- Length
- 552 residues
- Chains
- 7
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Like-sm ribonucleoprotein core
- UniProt
- D0KRQ0
- Pockets
- 3 · best druggability 0.43
Structure
x-ray diffraction · 5 distinct chains · 12% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Like-sm ribonucleoprotein core | protein | 78 | 14% helix, 40% strand | D0KRQ0 |
| B, C, E | Like-sm ribonucleoprotein core | protein | 77 | 8% helix, 49% strand | D0KRQ0 |
| D | Like-sm ribonucleoprotein core | protein | 79 | 11% helix, 48% strand | D0KRQ0 |
| F | Like-sm ribonucleoprotein core | protein | 83 | 12% helix, 48% strand | D0KRQ0 |
| G | Like-sm ribonucleoprotein core | protein | 81 | 16% helix, 43% strand | D0KRQ0 |
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 | 77 | 0.43 | 0.80 | 15 | empty |
| 2 | 71 | 0.35 | 0.77 | 14 | empty |
| 3 | 64 | 0.29 | 0.74 | 18 | empty |
Interfaces
7 interfaces between chains.
- F–G · 957 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 956 Ų buried · 11 hydrogen bonds · protein-protein
- A–G · 952 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 933 Ų buried · 17 hydrogen bonds · protein-protein
- D–E · 902 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 4XQ3 · Crystal structure of Sso-SmAP2 · the same entry in another collection · chain A against A, 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 D0KRQ0
- Elsewhere: RCSB PDB 4XQ3 · PDBe 4XQ3 · UniProt D0KRQ0
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