MolNFT v2 · #11165 · protein

Altered topology and flexibility in engineered subtilisin

1JEA: “Altered topology and flexibility in engineered subtilisin”. X-ray diffraction at 2, 2 ligands (CA, SO4), 1 pocket (best druggability 0.36). MolNFT v2 #11165 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1JEA
Type: protein
Length: 269 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2
Source: Bacillus lentus
Molecule: Subtilisin
EC: 3.4.21.62
UniProt: P29600
Ligands: CA, SO4
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction · resolution 2 · 1 distinct chain · 30% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Subtilisin (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	90	0.36	0.75	32	empty

Compared structures

1JEA · Altered topology and flexibility in engineered subtilisin · 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 1JEA · PDBe 1JEA · UniProt P29600

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