MolNFT v1 · #150701 · protein

Cold-adapted beta-D-galactosidase from arthrobacter sp. 32CB - data collected at room temperature

6H1P · Beta-galactosidase: “Cold-adapted beta-D-galactosidase from arthrobacter sp. 32CB - data collected at room temperature”. X-ray diffraction, 1 ligand (NA), 14 pockets (best druggability 0.66). MolNFT v1 #150701 on GenesisL1: 3D…

PDB: 6H1P
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
Ligands: NA
Pockets: 14 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-galactosidase (EC 3.2.1.23)	protein	989	15% helix, 37% strand	A0A023UGN9

Ligands and binding sites

NA · Sodium ion · metal · chains A

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

Pockets

14 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	210	0.66	0.85	27	empty
2	187	0.57	0.80	32	empty
3	76	0.53	0.86	23	empty
4	230	0.53	0.77	35	NA
5	85	0.50	0.84	22	empty

Compared structures

6H1P · Cold-adapted beta-D-galactosidase from Arthrobacter sp. 32cB - data collected at room… · 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 6H1P · PDBe 6H1P · UniProt A0A023UGN9

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