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Cold-adapted beta-D-galactosidase from arthrobacter sp. 32CB mutant D207A

Analyse Cold-adapted beta-D-galactosidase from arthrobacter sp. 32CB mutant D207A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ZJV
Type: protein
Length: 989 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-galactosidase
EC: 3.2.1.23
UniProt: A0A023UGN9
Pockets: 15 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-galactosidase (EC 3.2.1.23)	protein	989	16% helix, 38% strand	A0A023UGN9

Ligands and binding sites

MLI · Malonate ion · additive · chains A

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

Pockets

15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	185	0.63	0.84	26	empty
2	344	0.57	0.75	50	empty
3	217	0.56	0.78	34	empty
4	125	0.52	0.81	24	empty
5	93	0.52	0.84	19	empty

Compared structures

6ZJV · Cold-adapted beta-D-galactosidase from Arthrobacter sp. 32cB mutant D207A · the same entry in another collection · 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 A0A023UGN9
Elsewhere: RCSB PDB 6ZJV · PDBe 6ZJV · UniProt A0A023UGN9

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