MolNFT v1 · #6821 · protein

Crystal structure of beta-1,4-galactanase from aspergillus aculeatus at 100K

1FOB: “Crystal structure of beta-1,4-galactanase from aspergillus aculeatus at 100K”. X-ray diffraction, 1 ligand (CA), 1 pocket (best druggability 0.51). MolNFT v1 #6821 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1FOB
Type: protein
Length: 334 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-1,4-galactanase
EC: 3.2.1.89
UniProt: P48842
Ligands: CA
Pockets: 1 · best druggability 0.51

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-1,4-galactanase (EC 3.2.1.89)	protein	334	37% helix, 16% strand	P48842

Ligands and binding sites

CA · Calcium ion · metal

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	185	0.51	0.77	32	CA

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1FOB · Crystal structure of beta-1,4-galactanase from aspergillus aculeatus at 100K · the same entry in another collection · chain A against A, TM-score 1.00
P48842 · AlphaFold monomer V2.0 prediction for arabinogalactan endo- beta-1,4-galactanase (P48842) · 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 P48842
Elsewhere: RCSB PDB 1FOB · PDBe 1FOB · UniProt P48842

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