Research workbench
Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis
Analyse Contributions of engineered surface salt bridges to the stability of T4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1L37
- Type
- protein
- Length
- 164 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- T4 lysozyme
- EC
- 3.2.1.17
- UniProt
- P00720
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 64% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | T4 lysozyme (EC 3.2.1.17) | protein | 164 | 64% helix, 9% strand | P00720 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 268 | 0.53 | 0.76 | 31 | empty |
Compared structures
- 1L37 · Contributions of engineered surface salt bridges to the stability of T4 lysozyme… · 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 P00720
- Elsewhere: RCSB PDB 1L37 · PDBe 1L37 · UniProt P00720
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