Research workbench

Crystallization and structure determination of cytoplasm serine hydroxymethyltransferase (shmt) from pichia pastoris

Analyse Crystallization and structure determination of cytoplasm serine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5Z0Y
Type: protein
Length: 372 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Serine hydroxymethyltransferase
EC: 2.1.2.1
UniProt: F2QZA4
Pockets: 4 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serine hydroxymethyltransferase (EC 2.1.2.1)	protein	372	48% helix, 15% strand	F2QZA4

Ligands and binding sites

GOL · Glycerol · additive · chains A

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

Pockets

4 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	294	0.65	0.81	53	empty
2	74	0.38	0.77	16	empty
3	95	0.36	0.74	17	empty
4	53	0.32	0.77	13	empty

Compared structures

5Z0Y · Crystallization and structure determination of cytoplasm serine hydroxymethyltransferase… · 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 F2QZA4
Elsewhere: RCSB PDB 5Z0Y · PDBe 5Z0Y · UniProt F2QZA4

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.