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Cold-adapted beta-D-galactosidase from arthrobacter sp. 32CBON complex with onpg

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

PDB: 6SEC
Type: protein
Length: 988 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
Ligands: 145, NA
Pockets: 16 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-galactosidase (EC 3.2.1.23)	protein	988	16% helix, 37% strand	A0A023UGN9

Ligands and binding sites

145 · 2-nitrophenyl beta-D-galactopyranoside · ligand · chains A
NA · Sodium ion · metal · chains A
ACT · Acetate ion · additive · 2 copies · chains A

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

Pockets

16 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	185	0.63	0.84	29	empty
2	73	0.53	0.87	19	ACT
3	215	0.52	0.77	32	empty
4	101	0.52	0.83	21	empty
5	256	0.49	0.74	43	empty

Compared structures

6SEC · Cold-adapted beta-D-galactosidase from Arthrobacter sp. 32cBon complex with ONPG · 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 6SEC · PDBe 6SEC · UniProt A0A023UGN9

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