Research workbench
Crystal structure of bacterial serine phosphatase with his-tag mutation
Analyse Crystal structure of bacterial serine phosphatase with his-tag mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IHS
- Type
- protein
- Length
- 254 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphorylated protein phosphatase
- EC
- 3.1.3.16
- UniProt
- Q9RL81
- Ligands
- MG
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphorylated protein phosphatase (EC 3.1.3.16) | protein | 254 | 33% helix, 26% strand | Q9RL81 |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 171 | 0.56 | 0.81 | 23 | empty |
| 2 | 91 | 0.42 | 0.79 | 18 | MG |
| 3 | 80 | 0.34 | 0.75 | 22 | empty |
Compared structures
- 6IHS · Crystal structure of bacterial serine phosphatase with His-tag mutation · 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 Q9RL81
- Elsewhere: RCSB PDB 6IHS · PDBe 6IHS · UniProt Q9RL81
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