MolNFT v1 · #176588 · protein

Crystal structure of polysaccharide lyase ULY1

7DRQ: “Crystal structure of polysaccharide lyase ULY1”. X-ray diffraction, 1 ligand (CA), 10 pockets (best druggability 0.79). MolNFT v1 #176588 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7DRQ
Type: protein
Length: 960 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ULY1
UniProt: A0A0J8GWN9
Ligands: CA
Pockets: 10 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ULY1	protein	481	7% helix, 45% strand	A0A0J8GWN9
B	ULY1	protein	479	8% helix, 45% strand	A0A0J8GWN9

Ligands and binding sites

CA · Calcium ion · metal · 5 copies · chains A, B

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

Pockets

10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1168	0.79	0.81	106	empty
2	1064	0.77	0.79	80	empty
3	361	0.58	0.75	40	empty
4	153	0.50	0.79	27	empty
5	120	0.48	0.80	27	empty

Interfaces

1 interface between chains.

A–B · 569 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 modified (engineered).

Compared structures

7DRQ · Crystal structure of polysaccharide lyase Uly1 · 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 A0A0J8GWN9
Elsewhere: RCSB PDB 7DRQ · PDBe 7DRQ · UniProt A0A0J8GWN9

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