Research workbench
Crystal structure of human protein tyrosine phosphatase 4A1
Analyse Crystal structure of human protein tyrosine phosphatase 4A1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RXD
- Type
- protein
- Length
- 452 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein tyrosine phosphatase type iva, member 1
- UniProt
- Q93096
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Protein tyrosine phosphatase type iva, member 1 | protein | 150 | 43% helix, 17% strand | Q93096 |
| B | Protein tyrosine phosphatase type iva, member 1 | protein | 152 | 39% helix, 16% strand | Q93096 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 378 | 0.70 | 0.82 | 34 | empty |
| 2 | 91 | 0.30 | 0.72 | 16 | empty |
Interfaces
3 interfaces between chains.
- A–C · 645 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 641 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 632 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 modified, 3 disulfide (engineered, disulfide).
Compared structures
- 1RXD · Crystal structure of human protein tyrosine phosphatase 4A1 · the same entry in another collection · chain A against A, TM-score 1.00
- Q93096 · AlphaFold monomer V2.0 prediction for protein tyrosine phosphatase type iva 1 (Q93096) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q93096
- Elsewhere: RCSB PDB 1RXD · PDBe 1RXD · UniProt Q93096
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