Research workbench

GRP94 N-terminal domain bound to geldanamycin: effects of mutants 168- 169 ks-aa

Analyse GRP94 N-terminal domain bound to geldanamycin: effects of mutants 168- 169 ks-aa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ESA
Type: protein
Length: 220 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endoplasmin
UniProt: P41148
Ligands: GDM
Pockets: 2 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endoplasmin	protein	220	43% helix, 27% strand	P41148

Ligands and binding sites

GDM · Geldanamycin · ligand · chains A
PGE · Triethylene glycol · additive · 2 copies · chains A
PG4 · Tetraethylene glycol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	471	0.70	0.80	56	GDM
2	83	0.35	0.75	22	PG4, PGE

Compared structures

2ESA · GRP94 n-terminal domain bound to geldanamycin: effects of mutants 168-169 KS-AA · 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 0.85

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 2ESA · PDBe 2ESA · UniProt P41148

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.