Research workbench
Crystallographic structure of the mature ectodomain of the human receptor-type protein-tyrosine phosphatase ia-2 at 1.30 ångströms
Analyse Crystallographic structure of the mature ectodomain of the human receptor-type… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QT7
- Type
- protein
- Length
- 180 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor-type tyrosine-protein phosphatase-like N
- EC
- 3.1.3.48
- UniProt
- Q16849
- Ligands
- CA
- Pockets
- 1 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-type tyrosine-protein phosphatase-like N (EC 3.1.3.48) | protein | 89 | 40% helix, 29% strand | Q16849 |
| B | Receptor-type tyrosine-protein phosphatase-like N (EC 3.1.3.48) | protein | 91 | 40% helix, 29% strand | Q16849 |
Ligands and binding sites
- CA · Calcium ion · metal · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 116 | 0.54 | 0.83 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 563 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 2QT7 · Crystallographic structure of the mature ectodomain of the human receptor-type… · the same entry in another collection · chain A against A, TM-score 1.00
- Q16849 · AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase-like N… · 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 Q16849
- Elsewhere: RCSB PDB 2QT7 · PDBe 2QT7 · UniProt Q16849
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