Research workbench
Crystal structure of had phosphatase from thermococcus onnurineus
Analyse Crystal structure of had phosphatase from thermococcus onnurineus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4YGR
- Type
- protein
- Length
- 215 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hydrolase
- UniProt
- B6YTD6
- Ligands
- MG
- Pockets
- 1 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hydrolase | protein | 215 | 52% helix, 14% strand | B6YTD6 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
- NHE · 2-[N-cyclohexylamino]ethane sulfonic acid · additive · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 230 | 0.56 | 0.78 | 31 | NHE, MG |
Compared structures
- 4YGR · Crystal structure of HAD phosphatase from Thermococcus onnurineus · 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 B6YTD6
- Elsewhere: RCSB PDB 4YGR · PDBe 4YGR · UniProt B6YTD6
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