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Crystal structure of etda-treated bdbd (reduced)

Analyse Crystal structure of etda-treated bdbd (reduced) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3GHA
Type: protein
Length: 186 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Disulfide bond formation protein D
UniProt: O32218
Ligands: UNX

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Disulfide bond formation protein D	protein	186	53% helix, 12% strand	O32218

Ligands and binding sites

UNX · Unknown atom or ion · ion · chains A
EDO · 1,2-ethanediol · additive · chains A

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

Compared structures

3GHA · Crystal Structure of ETDA-treated BdbD (Reduced) · the same entry in another collection · chain A against A, TM-score 1.00
O32218 · AlphaFold monomer V2.0 prediction for disulfide bond formation protein D (O32218) · a predicted model of the same protein · 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 O32218
Elsewhere: RCSB PDB 3GHA · PDBe 3GHA · UniProt O32218

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