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Cell wall binding domain of the staphylococcal phage 2638A endolysin

Analyse Cell wall binding domain of the staphylococcal phage 2638A endolysin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7AQH
Type
protein
Length
744 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ORF007
UniProt
Q4ZD58
Pockets
8 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 56% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, D, C, G, H, B, E, FORF007protein930% helix, 56% strandQ4ZD58

Ligands and binding sites

  • EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains A, H, E, D, G

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

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13710.620.7837empty
23570.590.7739empty
31090.410.7618empty
4660.350.7714empty
5580.320.7512empty

Interfaces

11 interfaces between chains.

  • A–E · 493 Ų buried · 6 hydrogen bonds · protein-protein
  • C–G · 490 Ų buried · 4 hydrogen bonds · protein-protein
  • H–E · 488 Ų buried · 3 hydrogen bonds · protein-protein
  • D–G · 476 Ų buried · 3 hydrogen bonds · protein-protein
  • H–F · 474 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 7AQH · Cell wall binding domain of the Staphylococcal phage 2638A endolysin · the same entry in another collection · chain E against E, TM-score 1.00

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