Research workbench
Conservation of solvent-binding sites in 10 crystal forms of T4 lysozyme
Analyse Conservation of solvent-binding sites in 10 crystal forms of T4 lysozyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 150L
- Type
- protein
- Length
- 650 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- T4 lysozyme
- EC
- 3.2.1.17
- UniProt
- P00720
- Pockets
- 5 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 65% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | T4 lysozyme (EC 3.2.1.17) | protein | 164 | 65% helix, 9% strand | P00720 |
| B, C, D | T4 lysozyme (EC 3.2.1.17) | protein | 162 | 65% helix, 7% strand | P00720 |
Pockets
5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 945 | 0.77 | 0.79 | 91 | empty |
| 2 | 456 | 0.60 | 0.75 | 47 | empty |
| 3 | 503 | 0.58 | 0.73 | 41 | empty |
| 4 | 81 | 0.56 | 0.86 | 21 | empty |
| 5 | 55 | 0.51 | 0.87 | 17 | empty |
Interfaces
5 interfaces between chains.
- A–C · 667 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 662 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 201 Ų buried · 1 hydrogen bond · protein-protein
- C–D · 167 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 147 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 150L · Conservation of solvent-binding sites in 10 crystal forms 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 150L · PDBe 150L · UniProt P00720
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