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Crystal structure of gsh-bound CGRX2/C15S

Analyse Crystal structure of gsh-bound CGRX2/C15S in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4TR1
Type: protein
Length: 184 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutaredoxin 3
UniProt: A8MJH2
Ligands: GSH
Pockets: 1 · best druggability 0.55

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutaredoxin 3	protein	92	40% helix, 18% strand	A8MJH2
B	Glutaredoxin 3	protein	92	41% helix, 18% strand	A8MJH2

Ligands and binding sites

GSH · Glutathione · ligand · 2 copies · chains A, 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	286	0.55	0.76	29	GSH

Interfaces

1 interface between chains.

A–B · 82 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified, 1 covalent (covalent ligand, nonstandard, oxidation).

Compared structures

4TR1 · Crystal structure of GSH-bound cGrx2/C15S · 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 A8MJH2
Elsewhere: RCSB PDB 4TR1 · PDBe 4TR1 · UniProt A8MJH2

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