Research workbench
Crystal structure of the complex between human prl-2 phosphatase in reduced state and bateman domain of human CNNM3
Analyse Crystal structure of the complex between human prl-2 phosphatase in reduced… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5K22
- Type
- protein
- Length
- 305 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein tyrosine phosphatase type iva 2; Metal transporter CNNM3
- EC
- 3.1.3.48
- UniProt
- Q12974, Q8NE01
- Pockets
- 3 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein tyrosine phosphatase type iva 2 (EC 3.1.3.48) | protein | 156 | 41% helix, 15% strand | Q12974 |
| B | Metal transporter CNNM3 | protein | 149 | 37% helix, 26% strand | Q8NE01 |
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 | 186 | 0.46 | 0.75 | 29 | empty |
| 2 | 98 | 0.43 | 0.78 | 18 | empty |
| 3 | 80 | 0.35 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 698 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 5K22 · Crystal structure of the complex between human PRL-2 phosphatase in reduced state and… · the same entry in another collection · chain A against A, TM-score 1.00
- Q12974 · AlphaFold monomer V2.0 prediction for protein tyrosine phosphatase type iva 2 (Q12974) · a predicted model of the same protein · chain A against A, TM-score 0.97
- Q8NE01 · AlphaFold monomer V2.0 prediction for metal transporter CNNM3 (Q8NE01) · a predicted model of the same protein · chain B against A, TM-score 0.91
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 Q12974
- Every structure of UniProt Q8NE01
- Elsewhere: RCSB PDB 5K22 · PDBe 5K22 · UniProt Q12974 · UniProt Q8NE01
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