Research workbench
Structure of human sts-2 histidine phosphatase domain
Analyse Structure of human sts-2 histidine phosphatase domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WDI
- Type
- protein
- Length
- 524 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin-associated and SH3 domain-containing protein a
- UniProt
- P57075
- Ligands
- SO4
- Pockets
- 6 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquitin-associated and SH3 domain-containing protein a | protein | 264 | 36% helix, 15% strand | P57075 |
| B | Ubiquitin-associated and SH3 domain-containing protein a | protein | 260 | 38% helix, 15% strand | P57075 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1125 | 0.76 | 0.79 | 85 | SO4 |
| 2 | 158 | 0.47 | 0.76 | 29 | empty |
| 3 | 152 | 0.45 | 0.76 | 29 | empty |
| 4 | 106 | 0.43 | 0.77 | 16 | empty |
| 5 | 102 | 0.42 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 788 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 5WDI · Structure of Human Sts-2 histidine phosphatase domain · the same entry in another collection · chain A against A, TM-score 1.00
- P57075 · AlphaFold monomer V2.0 prediction for ubiquitin-associated and SH3 domain-containing… · a predicted model of the same protein · chain B 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 P57075
- Elsewhere: RCSB PDB 5WDI · PDBe 5WDI · UniProt P57075
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