Research workbench
Crystal structure of the apo form of Y74F mutant E. COLI tryptophanase
Analyse Crystal structure of the apo form of Y74F mutant E. COLI tryptophanase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2V1P
- Type
- protein
- Length
- 467 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trypthopanase
- EC
- 4.1.99.1
- UniProt
- P0A853
- Ligands
- MG, CL
- Pockets
- 4 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trypthopanase (EC 4.1.99.1) | protein | 467 | 45% helix, 14% strand | P0A853 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 284 | 0.62 | 0.80 | 30 | empty |
| 2 | 364 | 0.58 | 0.75 | 41 | empty |
| 3 | 303 | 0.55 | 0.75 | 39 | empty |
| 4 | 183 | 0.51 | 0.78 | 28 | empty |
Modifications
Observed in the structure: 2 modified (artifact).
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 P0A853
- Elsewhere: RCSB PDB 2V1P · PDBe 2V1P · UniProt P0A853
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