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Structure of tenebrio molitor larval alpha-amylase

Analyse Structure of tenebrio molitor larval alpha-amylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JAE
Type: protein
Length: 471 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-amylase
EC: 3.2.1.1
UniProt: P56634
Ligands: CA, CL
Pockets: 3 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-amylase (EC 3.2.1.1)	protein	471	28% helix, 25% strand	P56634

Ligands and binding sites

CA · Calcium ion · metal · chains A
CL · Chloride ion · ion · chains A

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

Pockets

3 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	286	0.56	0.76	27	empty
2	133	0.43	0.76	24	empty
3	70	0.33	0.76	17	empty

Modifications

Observed in the structure: 4 disulfide, 1 modified (disulfide, cyclization).

Compared structures

1JAE · Structure of tenebrio molitor larval alpha-amylase · the same entry in another collection · chain A against A, TM-score 1.00
P56634 · AlphaFold monomer V2.0 prediction for alpha-amylase (P56634) · 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 P56634
Elsewhere: RCSB PDB 1JAE · PDBe 1JAE · UniProt P56634

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