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Structure of the 2TEL crystallization module fused to T4 lysozyme with a helical linker.

Analyse Structure of the 2TEL crystallization module fused to T4 lysozyme with a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2QAR
Type
protein
Length
682 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
E80-telsam domain; Telsam domain; Lysozyme
EC
3.2.1.17
Ligands
NO3, NH4
Pockets
3 · best druggability 0.48

Structure

x-ray diffraction · 4 distinct chains · 58% helix, 3% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AE80-telsam domainprotein8651% helix, 0% strand—
B, ETelsam domainprotein9369% helix, 0% strand—
C, FLysozyme (EC 3.2.1.17)protein16360% helix, 7% strand—
DE80-telsam domainprotein8452% helix, 0% strand—

Ligands and binding sites

  • NO3 · Nitrate ion · ion · 8 copies · chains A, B, D, E
  • NH4 · Ammonium ion · ion · 2 copies · chains A, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12350.480.7435empty
22320.480.7429empty
3950.430.7820NO3

Interfaces

4 interfaces between chains.

  • A–B · 831 Ų buried · 16 hydrogen bonds · protein-protein
  • D–E · 714 Ų buried · 13 hydrogen bonds · protein-protein
  • B–C · 57 Ų buried · 2 hydrogen bonds · protein-protein
  • E–F · 56 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 2QAR · Structure of the 2TEL crystallization module fused to T4 lysozyme with a helical linker. · the same entry in another collection · chain A against A, TM-score 1.00

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