MolNFT v1 · #147087 · protein

Crystal structure of the dario rerio galectin-1-L2

6E20: “Crystal structure of the dario rerio galectin-1-L2”. X-ray diffraction, 3 ligands (NDG, GAL, MG), 2 pockets (best druggability 0.36). MolNFT v1 #147087 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6E20
Type: protein
Length: 265 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Galectin
UniProt: Q6TGN5
Ligands: NDG, GAL, MG
Pockets: 2 · best druggability 0.36

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 66% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Galectin	protein	132	0% helix, 66% strand	Q6TGN5
B	Galectin	protein	133	0% helix, 66% strand	Q6TGN5

Ligands and binding sites

NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · 2 copies · chains A, B
GAL · beta-D-galactopyranose · sugar · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	74	0.36	0.77	17	empty
2	56	0.26	0.73	15	empty

Interfaces

1 interface between chains.

A–B · 595 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (alkylation).

Compared structures

6E20 · Crystal structure of the Dario rerio galectin-1-L2 · 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 Q6TGN5
Elsewhere: RCSB PDB 6E20 · PDBe 6E20 · UniProt Q6TGN5

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