MolNFT v1 · #84859 · protein

High resolution structure of human galectin-7

3ZXF: “High resolution structure of human galectin-7”. X-ray diffraction, 2 pockets (best druggability 0.36). MolNFT v1 #84859 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3ZXF
Type: protein
Length: 273 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Galectin-7
UniProt: P47929
Pockets: 2 · best druggability 0.36

Structure

x-ray diffraction · 2 distinct chains · 2% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Galectin-7	protein	135	2% helix, 56% strand	P47929
B	Galectin-7	protein	138	2% helix, 52% strand	P47929

Ligands and binding sites

ACT · Acetate ion · additive · 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	70	0.36	0.78	17	empty
2	50	0.29	0.76	16	empty

Interfaces

1 interface between chains.

A–B · 858 Å² buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (oxidation).

Compared structures

3ZXF · High resolution structure of Human Galectin-7 · 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 0.98

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 3ZXF · PDBe 3ZXF · UniProt P47929

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