Research workbench

Effects of engineered salt bridges on the stability of subtilisin bpn'

Analyse Effects of engineered salt bridges on the stability of subtilisin bpn' in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1S02
Type: protein
Length: 275 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Subtilisin bpn'
EC: 3.4.21.14
UniProt: P00782
Ligands: CA, SO4
Pockets: 1 · best druggability 0.33

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Subtilisin bpn' (EC 3.4.21.14)	protein	275	30% helix, 20% strand	P00782

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	86	0.33	0.74	32	empty

Compared structures

1S02 · Effects of engineered salt bridges on the stability of subtilisin bpn' · the same entry in another collection · chain A against A, TM-score 1.00
P00782 · AlphaFold monomer V2.0 prediction for subtilisin bpn' (P00782) · 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 P00782
Elsewhere: RCSB PDB 1S02 · PDBe 1S02 · UniProt P00782

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