MolNFT v1 · #27691 · protein

S-adenosylmethionine synthetase (mat, ATP: L-methionine S- adenosyltransferase, E.C.2.5.1.6) in which met residues are replaced with selenomethionine residues (mse)

1XRB: “S-adenosylmethionine synthetase (mat, ATP: L-methionine S- adenosyltransferase, E.C.2.5.1.6) in which met…”. X-ray diffraction, 3 ligands (MG, K, PO4), 1 pocket (best druggability 0.28). MolNFT v1 #27691 on GenesisL1: 3D structure…

PDB: 1XRB
Type: protein
Length: 377 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: S-adenosylmethionine synthetase
EC: 2.5.1.6
UniProt: P04384
Ligands: MG, K, PO4
Pockets: 1 · best druggability 0.28

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	S-adenosylmethionine synthetase (EC 2.5.1.6)	protein	377	33% helix, 26% strand	P04384

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A
K · Potassium ion · metal · 2 copies · chains A
PO4 · Phosphate ion · ion · 2 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	56	0.28	0.75	14	empty

Modifications

Observed in the structure: 9 modified (engineered).

Compared structures

1XRB · S-adenosylmethionine synthetase (MAT, ATP: L-methionine S-adenosyltransferase… · 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 P04384
Elsewhere: RCSB PDB 1XRB · PDBe 1XRB · UniProt P04384

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