MolNFT v1 · #11674 · protein
Alternative structures of a sequence extended T4 lysozyme show that the highly conserved beta-sheet region has weak intrinsic folding propensity
1JTN: “Alternative structures of a sequence extended T4 lysozyme show that the highly conserved beta-sheet region…”. X-ray diffraction, 1 ligand (SO4), 4 pockets (best druggability 0.54). MolNFT v1 #11674 on GenesisL1: 3D structure…
- PDB
- 1JTN
- Type
- protein
- Length
- 351 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysozyme
- EC
- 3.2.1.17
- UniProt
- P00720
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 63% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lysozyme (EC 3.2.1.17) | protein | 177 | 64% helix, 8% strand | P00720 |
| B | Lysozyme (EC 3.2.1.17) | protein | 174 | 62% helix, 8% strand | P00720 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 360 | 0.54 | 0.73 | 31 | empty |
| 2 | 60 | 0.45 | 0.83 | 13 | empty |
| 3 | 218 | 0.45 | 0.73 | 27 | empty |
| 4 | 173 | 0.44 | 0.74 | 19 | SO4 |
Interfaces
1 interface between chains.
- A–B · 442 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1JTN · Alternative Structures of a Sequence Extended T4 Lysozyme Show that the Highly Conserved… · 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 1JTN · PDBe 1JTN · UniProt P00720
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