Research workbench
Crystal structure of SRPK1 in complex with SPHINX31
Analyse Crystal structure of SRPK1 in complex with SPHINX31 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MY8
- Type
- protein
- Length
- 355 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Srsf protein kinase 1,SRSF protein kinase 1
- EC
- 2.7.11.1
- UniProt
- Q96SB4
- Ligands
- RXZ
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Srsf protein kinase 1,SRSF protein kinase 1 (EC 2.7.11.1) | protein | 355 | 44% helix, 16% strand | Q96SB4 |
Ligands and binding sites
- RXZ · Sphinx31 · ligand · chains A
- EDO · 1,2-ethanediol · additive · 20 copies · chains A
- CIT · Citric acid · additive · chains A
- GOL · Glycerol · additive · chains A
- DMS · Dimethyl sulfoxide · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 555 | 0.71 | 0.80 | 59 | GOL, EDO, RXZ |
| 2 | 86 | 0.39 | 0.77 | 15 | empty |
| 3 | 109 | 0.38 | 0.75 | 18 | empty |
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 Q96SB4
- Elsewhere: RCSB PDB 5MY8 · PDBe 5MY8 · UniProt Q96SB4
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