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Crystal-structure of the N-terminal large GTPase domain of human guanylate binding protein 1 (HGBP1) in complex with non-hydrolysable GTP analogue gppnhp

Analyse Crystal-structure of the N-terminal large GTPase domain of human guanylate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BC9
Type: protein
Length: 294 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Interferon-induced guanylate-binding protein 1
UniProt: P32455
Ligands: GNP, MG
Pockets: 1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Interferon-induced guanylate-binding protein 1	protein	294	36% helix, 20% strand	P32455

Ligands and binding sites

GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	238	0.65	0.83	29	MG, GNP

Compared structures

2BC9 · Crystal-structure of the N-terminal large GTPase Domain of human Guanylate Binding… · 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 0.92

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 2BC9 · PDBe 2BC9 · UniProt P32455

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