MolNFT v1 · #31179 · protein

Structure of hydrolase (glycosidase)

2AMG · 1,4-alpha-D-glucan maltotetrahydrolase: “Structure of hydrolase (glycosidase)”. X-ray diffraction, 1 ligand (CA), 2 pockets (best druggability 0.56). MolNFT v1 #31179 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2AMG
Type: protein
Length: 415 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 1,4-alpha-D-glucan maltotetrahydrolase
EC: 3.2.1.60
UniProt: P13507
Ligands: CA
Pockets: 2 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	1,4-alpha-D-glucan maltotetrahydrolase (EC 3.2.1.60)	protein	415	36% helix, 17% strand	P13507

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	136	0.56	0.82	25	empty
2	244	0.56	0.77	33	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2AMG · Structure of hydrolase (glycosidase) · the same entry in another collection · chain A against A, TM-score 1.00
P13507 · AlphaFold monomer V2.0 prediction for glucan 1,4-alpha- maltotetraohydrolase (P13507) · 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 P13507
Elsewhere: RCSB PDB 2AMG · PDBe 2AMG · UniProt P13507

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