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Crystal structure of the protein-disulfide isomerase related chaperone ERP29

Analyse Crystal structure of the protein-disulfide isomerase related chaperone ERP29 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2QC7
Type: protein
Length: 448 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endoplasmic reticulum protein ERP29
UniProt: P30040
Pockets: 7 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Endoplasmic reticulum protein ERP29	protein	224	50% helix, 10% strand	P30040

Pockets

7 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	367	0.57	0.75	49	empty
2	86	0.41	0.78	20	empty
3	79	0.38	0.77	20	empty
4	85	0.35	0.75	21	empty
5	84	0.34	0.75	23	empty

Interfaces

1 interface between chains.

A–B · 183 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

2QC7 · Crystal structure of the protein-disulfide isomerase related chaperone ERp29 · the same entry in another collection · chain A against A, TM-score 1.00
P30040 · AlphaFold monomer V2.0 prediction for endoplasmic reticulum resident protein 29 (P30040) · 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 P30040
Elsewhere: RCSB PDB 2QC7 · PDBe 2QC7 · UniProt P30040

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