Research workbench
Crystal structure analysis of klebsiella sp ASR1 phytase
Analyse Crystal structure analysis of klebsiella sp ASR1 phytase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WU0
- Type
- protein
- Length
- 1,578 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phytase
- EC
- 3.1.3.8
- UniProt
- Q84CN9
- Ligands
- SO4
- Pockets
- 16 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Phytase (EC 3.1.3.8) | protein | 395 | 42% helix, 15% strand | Q84CN9 |
| B, D | Phytase (EC 3.1.3.8) | protein | 394 | 42% helix, 15% strand | Q84CN9 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 16 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 835 | 0.80 | 0.83 | 82 | SO4 |
| 2 | 469 | 0.67 | 0.79 | 43 | SO4 |
| 3 | 456 | 0.64 | 0.78 | 38 | SO4 |
| 4 | 451 | 0.64 | 0.78 | 42 | SO4 |
| 5 | 154 | 0.55 | 0.81 | 28 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1235 Ų buried · 22 hydrogen bonds · protein-protein
- A–D · 545 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 354 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 2WU0 · Crystal Structure Analysis of Klebsiella sp ASR1 Phytase · 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 Q84CN9
- Elsewhere: RCSB PDB 2WU0 · PDBe 2WU0 · UniProt Q84CN9
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