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The crystal structure of disulphide isomerase from xylella fastidiosa TEMECULA1

Analyse The crystal structure of disulphide isomerase from xylella fastidiosa TEMECULA1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3FK8
Type: protein
Length: 131 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Disulphide isomerase
UniProt: Q87CN2
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Disulphide isomerase	protein	131	46% helix, 16% strand	Q87CN2

Ligands and binding sites

FMT · Formic acid · additive · 4 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	60	0.37	0.79	14	empty

Modifications

Observed in the structure: 1 modified (engineered).

Compared structures

3FK8 · The crystal structure of disulphide isomerase from Xylella fastidiosa Temecula1 · the same entry in another collection · chain A against A, TM-score 1.00

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 Q87CN2
Elsewhere: RCSB PDB 3FK8 · PDBe 3FK8 · UniProt Q87CN2

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