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Human methionine adenosyltransferase 2A bound to methylthioadenosine and two sulfate in the active site

Analyse Human methionine adenosyltransferase 2A bound to methylthioadenosine and two… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7RXX
Type: protein
Length: 381 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P31153
Ligands: MTA, P3G, NA, MG, K, SO4

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	381	—	P31153

Ligands and binding sites

MTA · 5'-deoxy-5'-methylthioadenosine · ligand · chains A
P3G · 3,6,9,12,15-pentaoxaheptadecane · ligand · chains A
NA · Sodium ion · metal · 4 copies · chains A
MG · Magnesium ion · metal · 2 copies · chains A
K · Potassium ion · metal · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A
EDO · 1,2-ethanediol · additive · chains A

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

Compared structures

7RXX · Human Methionine Adenosyltransferase 2A bound to Methylthioadenosine and two sulfate in… · the same entry in another collection · chain A against A, TM-score 1.00
P31153 · AlphaFold monomer V2.0 prediction for S-adenosylmethionine synthase isoform type-2… · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P31153
Elsewhere: RCSB PDB 7RXX · PDBe 7RXX · UniProt P31153

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