Research workbench
Human receptor protein tyrosine phosphatase gamma, domain 1, in complex with vanadate, orthorhombic crystal form
Analyse Human receptor protein tyrosine phosphatase gamma, domain 1, in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QCC
- Type
- protein
- Length
- 568 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor-type tyrosine-protein phosphatase gamma
- EC
- 3.1.3.48
- UniProt
- P23470
- Ligands
- VO4
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-type tyrosine-protein phosphatase gamma (EC 3.1.3.48) | protein | 283 | 35% helix, 24% strand | P23470 |
| B | Receptor-type tyrosine-protein phosphatase gamma (EC 3.1.3.48) | protein | 285 | 36% helix, 22% strand | P23470 |
Ligands and binding sites
- VO4 · Vanadate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 423 | 0.80 | 0.88 | 47 | VO4 |
| 2 | 420 | 0.60 | 0.76 | 46 | empty |
| 3 | 74 | 0.32 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 645 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3QCC · Human receptor protein tyrosine phosphatase gamma, domain 1, in complex with vanadate… · the same entry in another collection · chain A against A, TM-score 1.00
- P23470 · AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase gamma… · 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 P23470
- Elsewhere: RCSB PDB 3QCC · PDBe 3QCC · UniProt P23470
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