Research workbench
Crystal structure of the G136F mutant of the first R-stereoselective - transaminase identified from arthrobacter sp. KNK168 (ferm-bp-5228)
Analyse Crystal structure of the G136F mutant of the first R-stereoselective… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WWI
- Type
- protein
- Length
- 3,864 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- (R)-amine transaminase
- EC
- 2.1.6.18
- UniProt
- F7J696
- Ligands
- PLP
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | (R)-amine transaminase (EC 2.1.6.18) | protein | 322 | 27% helix, 27% strand | F7J696 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 12 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 727 | 0.82 | 0.86 | 105 | empty |
| 2 | 844 | 0.80 | 0.83 | 107 | empty |
| 3 | 835 | 0.79 | 0.82 | 94 | PLP |
| 4 | 744 | 0.79 | 0.83 | 92 | PLP |
| 5 | 604 | 0.77 | 0.83 | 75 | PLP |
Interfaces
22 interfaces between chains.
- C–D · 2524 Ų buried · 49 hydrogen bonds · protein-protein
- G–J · 2517 Ų buried · 50 hydrogen bonds · protein-protein
- F–K · 2513 Ų buried · 48 hydrogen bonds · protein-protein
- H–I · 2507 Ų buried · 46 hydrogen bonds · protein-protein
- A–B · 2482 Ų buried · 46 hydrogen bonds · protein-protein
Compared structures
- 3WWI · Crystal structure of the G136F mutant of the first R-stereoselective -transaminase… · 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 F7J696
- Elsewhere: RCSB PDB 3WWI · PDBe 3WWI · UniProt F7J696
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