MolNFT v1 · #33078 · protein
Crystal structure of the mam-ig module of receptor protein tyrosine phosphatase mu
2C9A · Receptor-type tyrosine-protein phosphatase mu: “Crystal structure of the mam-ig module of receptor protein tyrosine phosphatase mu”. X-ray diffraction, 4 ligands (NAG, MAN, FUC), 1 pocket (best druggability 0.30). MolNFT v1 #33078…
- PDB
- 2C9A
- Type
- protein
- Length
- 259 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor-type tyrosine-protein phosphatase mu
- EC
- 3.1.3.48
- UniProt
- P28827
- Ligands
- NAG, MAN, FUC, NA
- Pockets
- 1 · best druggability 0.30
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-type tyrosine-protein phosphatase mu (EC 3.1.3.48) | protein | 259 | 3% helix, 47% strand | P28827 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
- MAN · alpha-D-mannopyranose · sugar · 2 copies
- FUC · alpha-L-fucopyranose · sugar
- NA · Sodium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.30 | 0.76 | 17 | empty |
Modifications
Observed in the structure: 3 disulfide, 3 glycan, 3 modified (disulfide, N-glycosylation, engineered).
Compared structures
- 2C9A · Crystal structure of the MAM-Ig module of receptor protein tyrosine phosphatase mu · the same entry in another collection · chain A against A, TM-score 1.00
- P28827 · AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase mu… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P28827
- Elsewhere: RCSB PDB 2C9A · PDBe 2C9A · UniProt P28827
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