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BioLiP

Structure of PDB 1mxa Chain A

Receptor sequence
>1mxaA (length=377) Species: 562 (Escherichia coli) [Search protein sequence]
AKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMV
LVGGEITTSAWVDIEEITRNTVREIGYVHSDMGFDANSCAVLSAIGKQSP
DRADPLEQGAGDQGLMFGYATNETDVLMPAPITYAHRLVQRQAEVRKNGT
LPWLRPDAKSQVTFQYDDGKIVGIDAVVLSTQHSEEIDQKSLQEAVMEEI
IKPILPAEWLTSATKFFINPTGRFVIGGPMGDCGLTGRKIIVDTYGGMAR
HGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQVSYAIGVAE
PTSIMVETFGTEKVPSEQLTLLVREFFDLRPYGLIQMLDLLHPIYKETAA
YGHFGREHFPWEKTDKAQLLRDAAGLK
3D structure
PDB1mxa Structure and function of S-adenosylmethionine synthetase: crystal structures of S-adenosylmethionine synthetase with ADP, BrADP, and PPi at 28 angstroms resolution.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1mxa, PDBe:1mxa, PDBj:1mxa
PDBsum1mxa
PubMed8611562
UniProtP0A817|METK_ECOLI S-adenosylmethionine synthase (Gene Name=metK)

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