Structure of PDB 1mxa Chain A

Receptor sequence

>1mxaA (length=377) Species: 562 (Escherichia coli)

AKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMV
LVGGEITTSAWVDIEEITRNTVREIGYVHSDMGFDANSCAVLSAIGKQSP
DRADPLEQGAGDQGLMFGYATNETDVLMPAPITYAHRLVQRQAEVRKNGT
LPWLRPDAKSQVTFQYDDGKIVGIDAVVLSTQHSEEIDQKSLQEAVMEEI
IKPILPAEWLTSATKFFINPTGRFVIGGPMGDCGLTGRKIIVDTYGGMAR
HGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQVSYAIGVAE
PTSIMVETFGTEKVPSEQLTLLVREFFDLRPYGLIQMLDLLHPIYKETAA
YGHFGREHFPWEKTDKAQLLRDAAGLK

3D structure

• PDB: 1mxa Structure and function of S-adenosylmethionine synthetase: crystal structures of S-adenosylmethionine synthetase with ADP, BrADP, and PPi at 28 angstroms resolution.
• Chain: A
• Resolution: 2.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H14 D16 K17 E42 E55 K165 F230 D238 C239 R244 K245 K265 K269 D271
• Catalytic site (residue number reindexed from 1): H14 D16 K17 E42 E55 K159 F224 D232 C233 R238 K239 K259 K263 D265
• Enzyme Commision number: 2.5.1.6: methionine adenosyltransferase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	PO4	A	A261 K265	A255 K259

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0004478 methionine adenosyltransferase activity
• GO:0005515 protein binding
• GO:0005524 ATP binding
• GO:0016740 transferase activity
• GO:0030955 potassium ion binding
• GO:0042802 identical protein binding
• GO:0046872 metal ion binding

Biological Process

• GO:0006556 S-adenosylmethionine biosynthetic process
• GO:0006730 one-carbon metabolic process
• GO:0033353 S-adenosylmethionine cycle

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:1mxa, PDBe:1mxa, PDBj:1mxa
• PDBsum: 1mxa
• PubMed: 8611562
• UniProt: P0A817|METK_ECOLI S-adenosylmethionine synthase (Gene Name=metK)