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The M23 peptidase domain of the staphylococcal phage 2638A endolysin

Analyse The M23 peptidase 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
6YJ1
Type
protein
Length
338 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ORF007
UniProt
Q4ZD58
Ligands
ZN
Pockets
2 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BORF007protein16911% helix, 34% strandQ4ZD58

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12600.700.8534empty
22720.690.8430empty

Interfaces

1 interface between chains.

  • A–B · 158 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 6YJ1 · The M23 peptidase domain of the Staphylococcal phage 2638A endolysin · the same entry in another collection · chain A against A, TM-score 1.00

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