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The complex structure of mutant phytase with ihs
Analyse The complex structure of mutant phytase with ihs in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4TSR
- Type
- protein
- Length
- 399 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Periplasmic appa protein
- EC
- 3.1.3.2, 3.1.3.26
- UniProt
- P07102
- Ligands
- IHS, NI
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Periplasmic appa protein (EC 3.1.3.2, 3.1.3.26) | protein | 399 | 43% helix, 15% strand | P07102 |
Ligands and binding sites
- IHS · D-myo-inositol-hexasulphate · ligand · chains A
- NI · Nickel (II) ion · metal · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 468 | 0.65 | 0.78 | 38 | NI, IHS |
| 2 | 51 | 0.30 | 0.76 | 18 | empty |
| 3 | 52 | 0.28 | 0.74 | 12 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
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 P07102
- Elsewhere: RCSB PDB 4TSR · PDBe 4TSR · UniProt P07102
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