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Use of sequence duplication to engineer a ligand-triggered long- distance molecular switch in T4 lysozyme

Analyse Use of sequence duplication to engineer a ligand-triggered long- distance… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1T97
Type
protein
Length
338 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lysozyme
EC
3.2.1.17
UniProt
P00720
Pockets
5 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 61% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALysozyme (EC 3.2.1.17)protein16561% helix, 8% strandP00720
BLysozyme (EC 3.2.1.17)protein17361% helix, 8% strandP00720

Pockets

5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12180.810.9431empty
22280.490.7530empty
32300.470.7328empty
4700.390.7818empty
5580.290.7417empty

Interfaces

1 interface between chains.

  • A–B · 903 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 1T97 · Use of sequence duplication to engineer a ligand-triggered long-distance molecular switch… · the same entry in another collection · chain A against A, TM-score 1.00

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