Research workbench
Crystal structure of the phosphatase SC4828 with the non-hydrolyzable nucleotide gpcp
Analyse Crystal structure of the phosphatase SC4828 with the non-hydrolyzable… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EXM
- Type
- protein
- Length
- 210 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatase SC4828
- EC
- 3.6.1.6
- UniProt
- Q9FBN7
- Ligands
- GP2, CA, NA
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatase SC4828 (EC 3.6.1.6) | protein | 210 | 20% helix, 39% strand | Q9FBN7 |
Ligands and binding sites
- GP2 · Phosphomethylphosphonic acid guanosyl ester · ligand · chains A
- CA · Calcium ion · metal · 3 copies · chains A
- NA · Sodium ion · metal · 2 copies · chains A
- GOL · Glycerol · additive · chains A
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 | 519 | 0.70 | 0.79 | 41 | CA, GP2 |
| 2 | 64 | 0.32 | 0.75 | 19 | empty |
Compared structures
- 3EXM · Crystal structure of the phosphatase SC4828 with the non-hydrolyzable nucleotide GPCP · the same entry in another collection · chain A against A, TM-score 1.00
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 Q9FBN7
- Elsewhere: RCSB PDB 3EXM · PDBe 3EXM · UniProt Q9FBN7
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