Research workbench

GRP1 pH domain (unliganded)

Analyse GRP1 pH domain (unliganded) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1FGZ
Type: protein
Length: 127 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GRP1
UniProt: O08967
Ligands: SO4
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GRP1	protein	127	13% helix, 37% strand	O08967

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	97	0.48	0.81	18	SO4

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

1FGZ · GRP1 pH domain (unliganded) · the same entry in another collection · chain A against A, TM-score 1.00
O08967 · AlphaFold monomer V2.0 prediction for cytohesin-3 (O08967) · a predicted model of the same protein · chain A against A, TM-score 0.91

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 O08967
Elsewhere: RCSB PDB 1FGZ · PDBe 1FGZ · UniProt O08967

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