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Crystal structure of the disulfide oxidoreductase dsba from proteus mirabilis

Analyse Crystal structure of the disulfide oxidoreductase dsba from proteus mirabilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4OCE
Type: protein
Length: 189 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: THIOL:DISULFIDE interchange protein
UniProt: B4EZ68
Pockets: 1 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	THIOL:DISULFIDE interchange protein	protein	189	49% helix, 11% strand	B4EZ68

Ligands and binding sites

MLI · Malonate ion · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	94	0.60	0.87	25	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4OCE · Crystal structure of the disulfide oxidoreductase DsbA from Proteus mirabilis · 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 B4EZ68
Elsewhere: RCSB PDB 4OCE · PDBe 4OCE · UniProt B4EZ68

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