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Crystal structure of complex between sa-subtilisin and tk-propeptide with deletion of the five C-terminal residues

Analyse Crystal structure of complex between sa-subtilisin and tk-propeptide with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3A3O
Type
protein
Length
378 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tk-subtilisin
EC
3.4.21.-
UniProt
P58502
Ligands
CA, ZN
Pockets
1 · best druggability 0.43

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATk-subtilisin (EC 3.4.21.-)protein31829% helix, 19% strandP58502
BTk-subtilisinprotein6030% helix, 40% strandP58502

Ligands and binding sites

  • CA · Calcium ion · metal · 7 copies · chains A
  • ZN · Zinc ion · metal · chains B

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
11110.430.7729empty

Interfaces

1 interface between chains.

  • A–B · 784 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 3A3O · Crystal structure of complex between SA-subtilisin and Tk-propeptide with deletion of the… · the same entry in another collection · chain A against A, TM-score 1.00
  • P58502 · AlphaFold monomer V2.0 prediction for tk-subtilisin (P58502) · a predicted model of the same protein · chain A against A, TM-score 1.00

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