Research workbench
Closed loop conformation of PHAZ7 Y105E mutant
Analyse Closed loop conformation of PHAZ7 Y105E mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MLY
- Type
- protein
- Length
- 684 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phb depolymerase PHAZ7
- UniProt
- Q939Q9
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Phb depolymerase PHAZ7 | protein | 342 | 27% helix, 17% strand | Q939Q9 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 114 | 0.39 | 0.75 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 258 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 5MLY · Closed loop conformation of PhaZ7 Y105E mutant · 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 Q939Q9
- Elsewhere: RCSB PDB 5MLY · PDBe 5MLY · UniProt Q939Q9
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