MolNFT v1 · #25304 · protein

Crystal structure of aminomethyltransferase (T protein; tetrahydrofolate-dependent) of glycine cleavage system (NP417381) from escherichia COLI K12 at 1.70 a resolution

1VLO: “Crystal structure of aminomethyltransferase (T protein; tetrahydrofolate-dependent) of glycine cleavage…”. X-ray diffraction, 1 pocket (best druggability 0.73). MolNFT v1 #25304 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 1VLO
Type: protein
Length: 364 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminomethyltransferase
EC: 2.1.2.10
UniProt: P27248
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aminomethyltransferase (EC 2.1.2.10)	protein	364	27% helix, 35% strand	P27248

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	443	0.73	0.83	64	empty

Modifications

Observed in the structure: 13 modified (engineered).

Compared structures

1VLO · Crystal structure of aminomethyltransferase (T protein; tetrahydrofolate-dependent) of… · the same entry in another collection · chain A against A, TM-score 1.00
P27248 · AlphaFold monomer V2.0 prediction for aminomethyltransferase (P27248) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P27248
Elsewhere: RCSB PDB 1VLO · PDBe 1VLO · UniProt P27248

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