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Crystal structure of T-protein of the glycine cleavage system

Analyse Crystal structure of T-protein of the glycine cleavage system in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WOS
Type: protein
Length: 361 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminomethyltransferase
EC: 2.1.2.10
UniProt: Q9WY54
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aminomethyltransferase (EC 2.1.2.10)	protein	361	25% helix, 36% strand	Q9WY54

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	526	0.72	0.81	63	empty
2	115	0.39	0.75	16	empty

Compared structures

1WOS · Crystal Structure of T-protein of the Glycine Cleavage System · the same entry in another collection · chain A against A, TM-score 1.00
Q9WY54 · AlphaFold monomer V2.0 prediction for aminomethyltransferase (Q9WY54) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q9WY54
Elsewhere: RCSB PDB 1WOS · PDBe 1WOS · UniProt Q9WY54

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