MolNFT v1 · #10738 · protein

Crystal structure of bacillus sp. GL1 xanthan lyase that acts on side chains of xanthan

1J0M: “Crystal structure of bacillus sp. GL1 xanthan lyase that acts on side chains of xanthan”. X-ray diffraction, 1 ligand (CA), 3 pockets (best druggability 0.77). MolNFT v1 #10738 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 1J0M
Type: protein
Length: 752 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Xanthan lyase
EC: 4.2.2.12
UniProt: Q9AQS0
Ligands: CA
Pockets: 3 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Xanthan lyase (EC 4.2.2.12)	protein	752	31% helix, 27% strand	Q9AQS0

Ligands and binding sites

CA · Calcium ion · metal · 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	1006	0.77	0.79	72	empty
2	172	0.45	0.75	31	empty
3	111	0.37	0.74	20	empty

Compared structures

1J0M · Crystal Structure of Bacillus sp. GL1 Xanthan Lyase that Acts on Side Chains of Xanthan · the same entry in another collection · chain A against A, TM-score 1.00
Q9AQS0 · AlphaFold monomer V2.0 prediction for xanthan lyase (Q9AQS0) · 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 Q9AQS0
Elsewhere: RCSB PDB 1J0M · PDBe 1J0M · UniProt Q9AQS0

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