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Crystal structure of human galectin-7 in complex with lactose

Analyse Crystal structure of human galectin-7 in complex with lactose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4GAL
Type: protein
Length: 270 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Galectin-7
UniProt: P47929
Ligands: BGC, GAL
Pockets: 3 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Galectin-7	protein	135	2% helix, 56% strand	P47929

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · chains B
GAL · beta-D-galactopyranose · sugar · chains B

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

Pockets

3 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	64	0.29	0.74	15	empty
2	54	0.28	0.74	16	empty
3	51	0.24	0.73	16	empty

Interfaces

1 interface between chains.

A–B · 829 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

4GAL · Crystal structure of human galectin-7 in complex with lactose · the same entry in another collection · chain A against A, TM-score 1.00
P47929 · AlphaFold monomer V2.0 prediction for galectin-7 (P47929) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P47929
Elsewhere: RCSB PDB 4GAL · PDBe 4GAL · UniProt P47929

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