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Structure of full length GRP94 with ADP bound

Analyse Structure of full length GRP94 with ADP bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2O1V
Type: protein
Length: 1,153 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endoplasmin
UniProt: P41148
Ligands: ADP, MG
Pockets: 19 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endoplasmin	protein	578	40% helix, 19% strand	P41148
B	Endoplasmin	protein	575	41% helix, 19% strand	P41148

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 4 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	648	0.78	0.83	72	empty
2	295	0.61	0.79	34	empty
3	281	0.61	0.79	32	empty
4	152	0.56	0.81	23	empty
5	213	0.53	0.77	19	empty

Interfaces

1 interface between chains.

A–B · 1736 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

2O1V · Structure of full length GRP94 with ADP bound · the same entry in another collection · chain A against A, TM-score 1.00
P41148 · AlphaFold monomer V2.0 prediction for endoplasmin (P41148) · a predicted model of the same protein · chain A against A, TM-score 0.74

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 P41148
Elsewhere: RCSB PDB 2O1V · PDBe 2O1V · UniProt P41148

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