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BETA1 domain-swapped structure of monothiol CGRX1(C16S)

Analyse BETA1 domain-swapped structure of monothiol CGRX1(C16S) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7C12
Type: protein
Length: 292 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutaredoxin
UniProt: A8MIN3
Pockets: 1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Glutaredoxin	protein	73	36% helix, 26% strand	A8MIN3

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	948	0.76	0.79	77	empty

Interfaces

5 interfaces between chains.

B–D · 1731 Å² buried · 34 hydrogen bonds · protein-protein
A–D · 778 Å² buried · 12 hydrogen bonds · protein-protein
B–C · 729 Å² buried · 7 hydrogen bonds · protein-protein
C–D · 229 Å² buried · 5 hydrogen bonds · protein-protein
A–B · 186 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

7C12 · beta1 domain-swapped structure of monothiol cGrx1(C16S) · 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 A8MIN3
Elsewhere: RCSB PDB 7C12 · PDBe 7C12 · UniProt A8MIN3

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