Research workbench

Crystal structure of oxidized GRX1

Analyse Crystal structure of oxidized GRX1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3C1R
Type: protein
Length: 110 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutaredoxin-1
EC: 1.20.4.1
UniProt: P25373

Structure

x-ray diffraction · 1 distinct chain · 58% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutaredoxin-1 (EC 1.20.4.1)	protein	110	58% helix, 16% strand	P25373

Ligands and binding sites

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

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

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3C1R · Crystal structure of oxidized GRX1 · the same entry in another collection · chain A against A, TM-score 1.00
P25373 · AlphaFold monomer V2.0 prediction for glutaredoxin-1 (P25373) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P25373
Elsewhere: RCSB PDB 3C1R · PDBe 3C1R · UniProt P25373

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.