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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: 1WOP
Type: protein
Length: 362 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminomethyltransferase
EC: 2.1.2.10
UniProt: Q9WY54
Ligands: FFO
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aminomethyltransferase (EC 2.1.2.10)	protein	362	26% helix, 37% strand	Q9WY54

Ligands and binding sites

FFO · N-[4-({[(6S)-2-amino-5-formyl-4-oxo-3,4,5,6,7,8-hexahydropteridin-6-yl]methyl}amino)benzoyl]-L-glutamic acid · ligand · 2 copies · chains A

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

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	529	0.72	0.80	70	FFO
2	121	0.41	0.75	15	FFO

Compared structures

1WOP · 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

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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 1WOP · PDBe 1WOP · UniProt Q9WY54

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