MolNFT v1 · #16847 · protein

Kinetic stabilization of bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface

1OB0: “Kinetic stabilization of bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at…”. X-ray diffraction, 2 ligands (CA, NA), 2 pockets (best druggability 0.51). MolNFT v1 #16847 on GenesisL1: 3D structure…

PDB: 1OB0
Type: protein
Length: 481 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-amylase
EC: 3.2.1.1
UniProt: P06278
Ligands: CA, NA
Pockets: 2 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-amylase (EC 3.2.1.1)	protein	481	27% helix, 24% strand	P06278

Ligands and binding sites

CA · Calcium ion · metal · 3 copies · chains A
NA · Sodium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	198	0.51	0.77	24	empty
2	50	0.24	0.72	22	empty

Compared structures

1OB0 · Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of… · the same entry in another collection · chain A against A, TM-score 1.00
P06278 · AlphaFold monomer V2.0 prediction for alpha-amylase (P06278) · 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 P06278
Elsewhere: RCSB PDB 1OB0 · PDBe 1OB0 · UniProt P06278

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.