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Structure of bacillus halmapalus alpha-amylase without any substrate analogues

Analyse Structure of bacillus halmapalus alpha-amylase without any substrate analogues in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2GJR
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: P19571
Ligands: CA, NA
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-amylase (EC 3.2.1.1)	protein	481	27% helix, 25% strand	P19571

Ligands and binding sites

CA · Calcium ion · metal · 3 copies · chains A
NA · Sodium ion · metal · chains A
ACT · Acetate ion · additive · 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	142	0.50	0.79	25	ACT

Compared structures

2GJR · Structure of bacillus halmapalus alpha-amylase without any substrate analogues · the same entry in another collection · chain A against A, TM-score 1.00
P19571 · AlphaFold monomer V2.0 prediction for glucan 1,4-alpha- maltohexaosidase (P19571) · 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 P19571
Elsewhere: RCSB PDB 2GJR · PDBe 2GJR · UniProt P19571

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