Research workbench

Thermoactinomyces vulgaris R-47 alpha-amylase 1 mutant enzyme W398V

Analyse Thermoactinomyces vulgaris R-47 alpha-amylase 1 mutant enzyme W398V in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1IZK
Type: protein
Length: 637 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amylase
EC: 3.2.1.1
UniProt: Q60053
Ligands: CA
Pockets: 4 · best druggability 0.68

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Amylase (EC 3.2.1.1)	protein	637	24% helix, 27% strand	Q60053

Ligands and binding sites

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

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

Pockets

4 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	285	0.68	0.83	42	empty
2	272	0.55	0.76	37	empty
3	60	0.39	0.80	20	empty
4	57	0.30	0.75	18	empty

Compared structures

1IZK · Thermoactinomyces vulgaris R-47 alpha-amylase 1 mutant enzyme w398v · the same entry in another collection · chain A against A, TM-score 1.00
Q60053 · AlphaFold monomer V2.0 prediction for neopullulanase 1 (Q60053) · 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 Q60053
Elsewhere: RCSB PDB 1IZK · PDBe 1IZK · UniProt Q60053

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