MolNFT v1 · #30313 · protein
Crystal structure of catalytic domain of human MAP kinase phosphatase 5
1ZZW · Dual specificity protein phosphatase 10: “Crystal structure of catalytic domain of human MAP kinase phosphatase 5”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.52). MolNFT v1 #30313 on GenesisL1: 3D structure…
- PDB
- 1ZZW
- Type
- protein
- Length
- 294 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity protein phosphatase 10
- EC
- 3.1.3.48, 3.1.3.16
- UniProt
- Q9Y6W6
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity protein phosphatase 10 (EC 3.1.3.48, 3.1.3.16) | protein | 147 | 46% helix, 16% strand | Q9Y6W6 |
| B | Dual specificity protein phosphatase 10 (EC 3.1.3.48, 3.1.3.16) | protein | 147 | 47% helix, 16% strand | Q9Y6W6 |
Ligands and binding sites
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 | 90 | 0.52 | 0.83 | 15 | EDO |
| 2 | 72 | 0.44 | 0.81 | 21 | empty |
| 3 | 51 | 0.40 | 0.82 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 437 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1ZZW · Crystal Structure of catalytic domain of Human MAP Kinase Phosphatase 5 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Y6W6 · AlphaFold monomer V2.0 prediction for dual specificity protein phosphatase 10 (Q9Y6W6) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9Y6W6
- Elsewhere: RCSB PDB 1ZZW · PDBe 1ZZW · UniProt Q9Y6W6
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