Research workbench
Structure of the phytase from citrobacter braakii at 2.3 ångström resolution.
Analyse Structure of the phytase from citrobacter braakii at 2.3 ångström resolution. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZHC
- Type
- protein
- Length
- 803 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phytase
- UniProt
- Q2VY22
- Ligands
- CL
- Pockets
- 11 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phytase | protein | 396 | 41% helix, 16% strand | Q2VY22 |
| B | Phytase | protein | 407 | 42% helix, 16% strand | Q2VY22 |
Ligands and binding sites
- CL · Chloride ion · ion · 10 copies · chains A, B
- FMT · Formic acid · additive · 16 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 530 | 0.77 | 0.84 | 70 | CL, FMT |
| 2 | 285 | 0.67 | 0.83 | 27 | FMT |
| 3 | 346 | 0.66 | 0.81 | 36 | FMT, CL |
| 4 | 322 | 0.59 | 0.78 | 35 | FMT, CL |
| 5 | 179 | 0.59 | 0.82 | 24 | FMT |
Interfaces
1 interface between chains.
- A–B · 1386 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 3ZHC · Structure of the phytase from Citrobacter braakii at 2.3 angstrom resolution. · 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 Q2VY22
- Elsewhere: RCSB PDB 3ZHC · PDBe 3ZHC · UniProt Q2VY22
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