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Crystal structure of the second catalytic domain of protein disulfide isomerase P5

Analyse Crystal structure of the second catalytic domain of protein disulfide isomerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4GWR
Type: protein
Length: 223 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein disulfide-isomerase A6
EC: 5.3.4.1
UniProt: Q15084
Pockets: 1 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein disulfide-isomerase A6 (EC 5.3.4.1)	protein	112	45% helix, 21% strand	Q15084
B	Protein disulfide-isomerase A6 (EC 5.3.4.1)	protein	111	45% helix, 21% strand	Q15084

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	179	0.62	0.83	34	empty

Interfaces

1 interface between chains.

A–B · 447 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

4GWR · Crystal Structure of the second catalytic domain of protein disulfide isomerase P5 · the same entry in another collection · chain A against A, TM-score 1.00
Q15084 · AlphaFold monomer V2.0 prediction for protein disulfide-isomerase A6 (Q15084) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 Q15084
Elsewhere: RCSB PDB 4GWR · PDBe 4GWR · UniProt Q15084

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