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Crystal structure of a cold adapted subtilisin-like serine proteinase

Analyse Crystal structure of a cold adapted subtilisin-like serine proteinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1SH7
Type
protein
Length
555 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Extracellular subtilisin-like serine proteinase
EC
3.4.21.-
UniProt
Q8GB52
Ligands
PMS, CA
Pockets
2 · best druggability 0.36

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AExtracellular subtilisin-like serine proteinase (EC 3.4.21.-)protein28126% helix, 22% strandQ8GB52
BExtracellular subtilisin-like serine proteinase (EC 3.4.21.-)protein27427% helix, 23% strandQ8GB52

Ligands and binding sites

  • PMS · phenylmethanesulfonic acid · ligand · 2 copies · chains A, B
  • CA · Calcium ion · metal · 6 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1920.360.7528PMS
21050.350.7432PMS

Modifications

Observed in the structure: 5 disulfide, 2 covalent (disulfide, covalent ligand).

Compared structures

  • 1SH7 · Crystal structure of a cold adapted subtilisin-like serine proteinase · the same entry in another collection · chain A against A, TM-score 1.00

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