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The structure of mall mutant enzyme G202P from bacillus subtilus

Analyse The structure of mall mutant enzyme G202P from bacillus subtilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4MB1
Type: protein
Length: 557 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Oligo-1,6-glucosidase 1
EC: 3.2.1.10
UniProt: O06994
Ligands: CA
Pockets: 3 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Oligo-1,6-glucosidase 1 (EC 3.2.1.10)	protein	557	33% helix, 18% strand	O06994

Ligands and binding sites

CA · Calcium ion · metal · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 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	637	0.80	0.85	63	TRS
2	74	0.36	0.77	19	empty
3	72	0.30	0.74	18	empty

Compared structures

4MB1 · The Structure of MalL mutant enzyme G202P from Bacillus subtilus · the same entry in another collection · chain A against A, TM-score 1.00
O06994 · AlphaFold monomer V2.0 prediction for oligo-1,6-glucosidase 1 (O06994) · 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 O06994
Elsewhere: RCSB PDB 4MB1 · PDBe 4MB1 · UniProt O06994

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