Research workbench
Native apha class B acid PHOSPHATASE/PHOSPHOTRANSFERASE from E. COLI
Analyse Native apha class B acid PHOSPHATASE/PHOSPHOTRANSFERASE from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CZ4
- Type
- protein
- Length
- 209 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Class B acid phosphatase
- EC
- 3.1.3.2
- UniProt
- P0AE22
- Ligands
- MG, CL
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Class B acid phosphatase (EC 3.1.3.2) | protein | 209 | 37% helix, 16% strand | P0AE22 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A
- CL · Chloride ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 5 copies · chains A
- ACT · Acetate ion · additive · 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 | 228 | 0.55 | 0.78 | 31 | ACT |
Compared structures
- 3CZ4 · Native AphA class B acid phosphatase/phosphotransferase from E. coli · the same entry in another collection · chain A against A, TM-score 1.00
- P0AE22 · AlphaFold monomer V2.0 prediction for class B acid phosphatase (P0AE22) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P0AE22
- Elsewhere: RCSB PDB 3CZ4 · PDBe 3CZ4 · UniProt P0AE22
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