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Crystal structure of human guanylate-binding protein 2 (HGBP2) K51A mutant

Analyse Crystal structure of human guanylate-binding protein 2 (HGBP2) K51A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7M1S
Type: protein
Length: 577 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Guanylate-binding protein 2
EC: 3.6.5.-
UniProt: P32456
Ligands: PO4
Pockets: 8 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 60% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Guanylate-binding protein 2 (EC 3.6.5.-)	protein	577	60% helix, 10% strand	P32456

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A

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

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	672	0.71	0.78	73	empty
2	279	0.61	0.79	26	empty
3	211	0.47	0.75	38	PO4
4	154	0.45	0.76	31	empty
5	56	0.44	0.83	15	empty

Compared structures

7M1S · Crystal structure of human guanylate-binding protein 2 (hGBP2) K51A mutant · the same entry in another collection · chain A against A, TM-score 1.00
P32456 · AlphaFold monomer V2.0 prediction for guanylate-binding protein 2 (P32456) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P32456
Elsewhere: RCSB PDB 7M1S · PDBe 7M1S · UniProt P32456

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