Research workbench
Tandem ig repeats of dlar
Analyse Tandem ig repeats of dlar in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PXJ
- Type
- protein
- Length
- 779 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein phosphatase lar
- EC
- 3.1.3.48
- UniProt
- P16621
- Pockets
- 3 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 2% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Tyrosine-protein phosphatase lar (EC 3.1.3.48) | protein | 199 | 2% helix, 52% strand | P16621 |
| C | Tyrosine-protein phosphatase lar (EC 3.1.3.48) | protein | 187 | 2% helix, 54% strand | P16621 |
| D | Tyrosine-protein phosphatase lar (EC 3.1.3.48) | protein | 194 | 2% helix, 51% strand | P16621 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1080 | 0.82 | 0.83 | 126 | empty |
| 2 | 1028 | 0.81 | 0.82 | 109 | empty |
| 3 | 112 | 0.39 | 0.75 | 17 | empty |
Interfaces
5 interfaces between chains.
- A–D · 1124 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 1114 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 166 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 120 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 12 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 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 P16621
- Elsewhere: RCSB PDB 3PXJ · PDBe 3PXJ · UniProt P16621
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