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Bacillus lentus subtilisin K27R/N87S/V104Y/N123S/T274A variant

Analyse Bacillus lentus subtilisin K27R/N87S/V104Y/N123S/T274A variant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1C9J
Type: protein
Length: 269 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Serine protease
EC: 3.4.21.62
UniProt: P29600
Ligands: CA, SO4
Pockets: 1 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serine protease (EC 3.4.21.62)	protein	269	30% helix, 20% strand	P29600

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A
SO4 · Sulfate ion · ion · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	89	0.32	0.73	28	empty

Compared structures

1C9J · Bacillus lentus subtilisin K27R/N87S/V104Y/N123S/T274A variant · the same entry in another collection · chain A against A, TM-score 1.00
P29600 · AlphaFold monomer V2.0 prediction for subtilisin savinase (P29600) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P29600
Elsewhere: RCSB PDB 1C9J · PDBe 1C9J · UniProt P29600

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