Research workbench
Crystal structure of the bro domain of hd-ptp
Analyse Crystal structure of the bro domain of hd-ptp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CRU
- Type
- protein
- Length
- 1,434 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein phosphatase non-receptor type 23
- EC
- 3.1.3.48
- UniProt
- Q9H3S7
- Pockets
- 15 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 66% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Tyrosine-protein phosphatase non-receptor type 23 (EC 3.1.3.48) | protein | 360 | 66% helix, 4% strand | Q9H3S7 |
| B, D | Tyrosine-protein phosphatase non-receptor type 23 (EC 3.1.3.48) | protein | 357 | 66% helix, 3% strand | Q9H3S7 |
Pockets
15 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 977 | 0.81 | 0.82 | 100 | empty |
| 2 | 1028 | 0.77 | 0.79 | 102 | empty |
| 3 | 1008 | 0.73 | 0.76 | 89 | empty |
| 4 | 225 | 0.62 | 0.81 | 27 | empty |
| 5 | 185 | 0.47 | 0.76 | 30 | empty |
Interfaces
4 interfaces between chains.
- B–D · 745 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 745 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 704 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 268 Ų buried · 2 hydrogen bonds · protein-protein
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 Q9H3S7
- Elsewhere: RCSB PDB 5CRU · PDBe 5CRU · UniProt Q9H3S7
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