MolNFT v1 · #25821 · protein

X-ray crystal structure of R111H human galectin-1

1W6Q: “X-ray crystal structure of R111H human galectin-1”. X-ray diffraction, 2 pockets (best druggability 0.49). MolNFT v1 #25821 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1W6Q
Type: protein
Length: 268 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Galectin-1
UniProt: P09382
Pockets: 2 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 64% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Galectin-1	protein	134	0% helix, 64% strand	P09382

Ligands and binding sites

BME · Beta-mercaptoethanol · additive · 6 copies · chains A, B

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	116	0.49	0.80	19	empty
2	86	0.45	0.80	18	empty

Interfaces

1 interface between chains.

A–B · 634 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 covalent, 1 modified (additive adduct, oxidation).

Compared structures

1W6Q · X-ray crystal structure of R111H human galectin-1 · the same entry in another collection · chain A against A, TM-score 1.00
P09382 · AlphaFold monomer V2.0 prediction for galectin-1 (P09382) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P09382
Elsewhere: RCSB PDB 1W6Q · PDBe 1W6Q · UniProt P09382

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