Research workbench
Crystal structure of human pseudouridylate synthase 7
Analyse Crystal structure of human pseudouridylate synthase 7 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5KKP
- Type
- protein
- Length
- 509 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pseudouridylate synthase 7
- EC
- 5.4.99.-
- UniProt
- Q96PZ0
- Ligands
- UNX
- Pockets
- 4 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pseudouridylate synthase 7 (EC 5.4.99.-) | protein | 509 | 37% helix, 21% strand | Q96PZ0 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 286 | 0.57 | 0.77 | 32 | EDO, UNX |
| 2 | 187 | 0.48 | 0.76 | 22 | empty |
| 3 | 161 | 0.41 | 0.73 | 23 | empty |
| 4 | 55 | 0.27 | 0.74 | 11 | empty |
Modifications
Observed in the structure: 15 modified (engineered).
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 Q96PZ0
- Elsewhere: RCSB PDB 5KKP · PDBe 5KKP · UniProt Q96PZ0
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