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Crystal structure of alkaline serine protease kp-43 from bacillus sp. ksm-KP43 (1.30 ångström, 100 K)

Analyse Crystal structure of alkaline serine protease kp-43 from bacillus sp. ksm-KP43… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1WMD
Type
protein
Length
434 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protease
EC
3.4.21.-
UniProt
Q93UV9
Ligands
CA, SO4
Pockets
2 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtease (EC 3.4.21.-)protein43421% helix, 26% strandQ93UV9

Ligands and binding sites

  • CA · Calcium ion · metal · 3 copies · chains A
  • SO4 · Sulfate ion · ion · chains A
  • DIO · 1,4-diethylene dioxide · additive · 2 copies · chains A
  • GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11100.370.7428DIO
2550.260.7318empty

Compared structures

  • 1WMD · Crystal Structure of alkaline serine protease KP-43 from Bacillus sp. KSM-KP43 (1.30… · the same entry in another collection · chain A against A, TM-score 1.00

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