MolNFT v1 · #165281 · protein
Crystal structures of fniii domain one and two of the human leucocyte common antigen-related protein, lar
6TPV · Receptor-type tyrosine-protein phosphatase F: “Crystal structures of fniii domain one and two of the human leucocyte common antigen-related protein, lar”. X-ray diffraction, 2 pockets (best druggability 0.58). MolNFT v1 #165281 on…
- PDB
- 6TPV
- Type
- protein
- Length
- 387 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor-type tyrosine-protein phosphatase F
- EC
- 3.1.3.48
- UniProt
- P10586
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-type tyrosine-protein phosphatase F (EC 3.1.3.48) | protein | 191 | 2% helix, 48% strand | P10586 |
| B | Receptor-type tyrosine-protein phosphatase F (EC 3.1.3.48) | protein | 196 | 2% helix, 47% strand | P10586 |
Ligands and binding sites
- IMD · Imidazole · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 317 | 0.58 | 0.77 | 36 | empty |
| 2 | 122 | 0.40 | 0.75 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 259 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6TPV · Crystal structures of FNIII domain one and two of the human leucocyte common… · the same entry in another collection · chain A against A, TM-score 1.00
- P10586 · AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase F… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P10586
- Elsewhere: RCSB PDB 6TPV · PDBe 6TPV · UniProt P10586
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