MolNFT v1 · #51956 · protein

Structure of N341ABSSHMT crystallized in the presence of L- allo-thr

2VMQ · Serine hydroxymethyltransferase: “Structure of N341ABSSHMT crystallized in the presence of L- allo-thr”. X-ray diffraction, 3 ligands (GLY, PLP, PO4), 2 pockets (best druggability 0.51). MolNFT v1 #51956 on GenesisL1: 3D structure…

PDB: 2VMQ
Type: protein
Length: 405 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Serine hydroxymethyltransferase
EC: 2.1.2.1
UniProt: Q7SIB6
Ligands: GLY, PLP, PO4
Pockets: 2 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serine hydroxymethyltransferase (EC 2.1.2.1)	protein	405	50% helix, 14% strand	Q7SIB6

Ligands and binding sites

GLY · Glycine · ligand · chains A
PLP · Pyridoxal-5'-phosphate · ligand · chains A
PO4 · Phosphate ion · ion · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 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	234	0.51	0.76	38	GLY, PLP
2	112	0.38	0.74	15	empty

Compared structures

2VMQ · Structure of N341AbsSHMT crystallized in the presence of L-allo-Thr · 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 Q7SIB6
Elsewhere: RCSB PDB 2VMQ · PDBe 2VMQ · UniProt Q7SIB6

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