MolNFT v1 · #63410 · protein
Evaulaution at atomic resolution of the role of strain in destabilizing the temperature sensitive T4 lysozyme mutant ARG96-- >his
3F8V: “Evaulaution at atomic resolution of the role of strain in destabilizing the temperature sensitive T4 lysozyme…”. X-ray diffraction, 4 ligands (NA, K, CL), 1 pocket (best druggability 0.50). MolNFT v1 #63410 on GenesisL1: 3D…
- PDB
- 3F8V
- Type
- protein
- Length
- 164 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysozyme
- EC
- 3.2.1.17
- UniProt
- P00720
- Ligands
- NA, K, CL, PO4
- Pockets
- 1 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lysozyme (EC 3.2.1.17) | protein | 164 | 62% helix, 8% strand | P00720 |
Ligands and binding sites
- NA · Sodium ion · metal · chains A
- K · Potassium ion · metal · chains A
- CL · Chloride ion · ion · 2 copies · chains A
- PO4 · Phosphate ion · ion · chains A
- HED · 2-hydroxyethyl disulfide · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 196 | 0.50 | 0.76 | 25 | NA |
Compared structures
- 3F8V · Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature… · 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 3F8V · PDBe 3F8V · UniProt P00720
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