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Structure of plyl

Analyse Structure of plyl in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1YB0
Type
protein
Length
473 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Prophage LAMBDABA02, N-acetylmuramoyl-L-alanine amidase, family 2
UniProt
Q81WA9
Ligands
ZN, PO4
Pockets
2 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CProphage LAMBDABA02, N-acetylmuramoyl-L-alanine amidase, family 2protein15742% helix, 17% strandQ81WA9
BProphage LAMBDABA02, N-acetylmuramoyl-L-alanine amidase, family 2protein15942% helix, 16% strandQ81WA9

Ligands and binding sites

  • ZN · Zinc ion · metal · 3 copies · chains A, B, C
  • PO4 · Phosphate ion · ion · 3 copies · chains A, B, C

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
16070.660.7677ZN, PO4
22510.550.7731ZN, PO4

Interfaces

3 interfaces between chains.

  • A–B · 372 Ų buried · 5 hydrogen bonds · protein-protein
  • B–C · 355 Ų buried · 4 hydrogen bonds · protein-protein
  • A–C · 341 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 1YB0 · Structure of PlyL · the same entry in another collection · chain A against A, TM-score 1.00

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