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Crystal structure of non-specific class-C acid phosphatase from sphingobium sp. rsms bound to bis-tris at pH 5.5
Analyse Crystal structure of non-specific class-C acid phosphatase from sphingobium sp.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7F7B
- Type
- protein
- Length
- 253 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acid phosphatase
- UniProt
- A0A197BYF0
- Ligands
- MG, PO4
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acid phosphatase | protein | 253 | 43% helix, 17% strand | A0A197BYF0 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
- PO4 · Phosphate ion · ion · chains A
- BTB · 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol · 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 | 381 | 0.59 | 0.76 | 31 | BTB, MG, PO4 |
| 2 | 234 | 0.50 | 0.75 | 19 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 7F7B · Crystal structure of Non-specific class-C acid phosphatase from Sphingobium sp. RSMS… · 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 A0A197BYF0
- Elsewhere: RCSB PDB 7F7B · PDBe 7F7B · UniProt A0A197BYF0
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