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Crystal structure of farnesylated HGBP1

Analyse Crystal structure of farnesylated HGBP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6K1Z
Type: protein
Length: 544 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Guanylate-binding protein 1
EC: 3.6.5.-
UniProt: P32455
Ligands: FAR
Pockets: 7 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 63% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Guanylate-binding protein 1 (EC 3.6.5.-)	protein	544	63% helix, 11% strand	P32455

Ligands and binding sites

FAR · Farnesyl · ligand · chains A

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

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	547	0.75	0.82	51	empty
2	187	0.66	0.85	30	empty
3	200	0.57	0.80	21	FAR
4	145	0.55	0.82	24	empty
5	121	0.47	0.79	21	empty

Modifications

Observed in the structure: 1 lipid (farnesylation).

Compared structures

6K1Z · Crystal structure of farnesylated hGBP1 · the same entry in another collection · chain A against A, TM-score 1.00
P32455 · AlphaFold monomer V2.0 prediction for guanylate-binding protein 1 (P32455) · 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 P32455
Elsewhere: RCSB PDB 6K1Z · PDBe 6K1Z · UniProt P32455

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