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Solution structure of the GCV_H domain from mouse glycine

Analyse Solution structure of the GCV_H domain from mouse glycine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2EDG
Type: protein
Length: 130 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycine cleavage system H protein
UniProt: Q91WK5
Pockets: 1 · best druggability 0.45

Structure

solution nmr · 1 distinct chain · 18% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycine cleavage system H protein	protein	130	18% helix, 35% strand	Q91WK5

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	73	0.45	0.81	16	empty

Compared structures

2EDG · Solution structure of the GCV_H domain from mouse glycine · the same entry in another collection · chain A against A, TM-score 1.00
Q91WK5 · AlphaFold monomer V2.0 prediction for glycine cleavage system H protein, mitochondrial… · a predicted model of the same protein · chain A against A, TM-score 0.93

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 Q91WK5
Elsewhere: RCSB PDB 2EDG · PDBe 2EDG · UniProt Q91WK5

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