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Isolated sbd of bip with LOOP34 modification

Analyse Isolated sbd of bip with LOOP34 modification in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5E86
Type: protein
Length: 230 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 78 kda glucose-regulated protein
UniProt: P11021
Pockets: 3 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	78 kda glucose-regulated protein	protein	230	40% helix, 25% strand	P11021

Pockets

3 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	134	0.56	0.82	24	empty
2	136	0.43	0.76	26	empty
3	77	0.41	0.80	20	empty

Compared structures

5E86 · isolated SBD of BiP with loop34 modification · the same entry in another collection · chain A against A, TM-score 1.00
P11021 · AlphaFold monomer V2.0 prediction for endoplasmic reticulum chaperone bip (P11021) · a predicted model of the same protein · chain A against A, TM-score 0.46

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 P11021
Elsewhere: RCSB PDB 5E86 · PDBe 5E86 · UniProt P11021

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