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Refined structure of alpha-lytic protease at 1.7 ångströms resolution. analysis of hydrogen bonding and solvent structure

Analyse Refined structure of alpha-lytic protease at 1.7 ångströms resolution. analysis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2ALP
Type
protein
Length
198 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-lytic protease
EC
3.4.21.12
UniProt
P00778
Ligands
SO4
Pockets
1 · best druggability 0.28

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 55% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha-lytic protease (EC 3.4.21.12)protein1987% helix, 55% strandP00778

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1560.280.7520SO4

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 2ALP · Refined structure of alpha-lytic protease at 1.7 ångströms resolution. analysis of… · the same entry in another collection · chain A against A, TM-score 1.00
  • P00778 · AlphaFold monomer V2.0 prediction for alpha-lytic protease (P00778) · a predicted model of the same protein · chain A against A, TM-score 1.00

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