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Crystal structure of ampylated GRP78 in apo form (crystal form 1)

Analyse Crystal structure of ampylated GRP78 in apo form (crystal form 1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6EOB
Type: protein
Length: 520 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 78 kda glucose-regulated protein
UniProt: G3I8R9
Ligands: PO4
Pockets: 3 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	78 kda glucose-regulated protein	protein	520	31% helix, 32% strand	G3I8R9

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

3 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	296	0.71	0.85	41	PO4
2	264	0.58	0.79	39	empty
3	77	0.30	0.73	15	empty

Compared structures

6EOB · Crystal structure of AMPylated GRP78 in apo form (Crystal form 1) · the same entry in another collection · chain A against A, TM-score 1.00
G3I8R9 · AlphaFold monomer V2.0 prediction for endoplasmic reticulum chaperone bip (G3I8R9) · 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 G3I8R9
Elsewhere: RCSB PDB 6EOB · PDBe 6EOB · UniProt G3I8R9

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