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Crystal structure of the protein disulfide bond isomerase, dsbc, from escherichia COLI

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

PDB: 1EEJ
Type: protein
Length: 432 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: THIOL:DISULFIDE interchange protein
EC: 5.3.4.1
UniProt: P21892
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	THIOL:DISULFIDE interchange protein (EC 5.3.4.1)	protein	216	38% helix, 23% strand	P21892

Ligands and binding sites

MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains B

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	88	0.36	0.75	18	empty

Interfaces

1 interface between chains.

A–B · 868 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1EEJ · Crystal structure of the protein disulfide bond isomerase, dsbc, from escherichia COLI · 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 P21892
Elsewhere: RCSB PDB 1EEJ · PDBe 1EEJ · UniProt P21892

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