Research workbench
Crystal of prl-1 complexed with peptide
Analyse Crystal of prl-1 complexed with peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RZ2
- Type
- protein
- Length
- 322 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein tyrosine phosphatase type iva 1; Prl-1 (PTP4A1)
- EC
- 3.1.3.48
- UniProt
- Q78EG7
- Pockets
- 2 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein tyrosine phosphatase type iva 1 (EC 3.1.3.48) | protein | 152 | 38% helix, 16% strand | Q78EG7 |
| C, D | Prl-1 (PTP4A1) | protein | 9 | 0% helix, 0% strand | — |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 73 | 0.63 | 0.91 | 20 | empty |
| 2 | 204 | 0.53 | 0.77 | 36 | empty |
Interfaces
3 interfaces between chains.
- A–C · 427 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 397 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 338 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 Q78EG7
- Elsewhere: RCSB PDB 3RZ2 · PDBe 3RZ2 · UniProt Q78EG7
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