Structure of PDB 6vcy Chain A

Receptor sequence
>6vcyA (length=385) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
METFLFTSESVNEGHPDKLCDQISDAVLDACLEQDPDSKVACETCTKTNM
VMVFGEITTKATVDYEKIVRDTCRAIGFVSDDVGLDADKCKVLVNIEQQS
PDIAQGVKCPEEIGAGDQGHMFGYATDETPELMPLSHVLATKLGARLTEV
RKNGTCAWLRPDGKTQVTVEYYNDKGAMVPIRVHTVLISTQHDETVTNDE
IARDLKEHVIKPVIPEKYLDEKTIFHLNPSGRFVIGGPHGDAGLTGRKII
IDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSVVANGMARRALVQ
VSYAIGVPEPLSVFVDTYETGLIPDKEILKIVKESFDFRPGMMTINLDLK
RGGNGRFLKTAAYGHFGRDDPDFTWEVVKPLKWDK
3D structure
PDB6vcy S-adenosylmethionine synthases in plants: Structural characterization of type I and II isoenzymes from Arabidopsis thaliana and Medicago truncatula.
ChainA
Resolution1.82 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H15 D17 K18 E43 E56 K169 F238 D246 A247 R252 K253 K273 K277 D279
Catalytic site (residue number reindexed from 1) H15 D17 K18 E43 E56 K164 F233 D241 A242 R247 K248 K268 K272 D274
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 MTA A H15 D167 S235 F238 D246 H15 D162 S230 F233 D241
Gene Ontology
Molecular Function
GO:0004478 methionine adenosyltransferase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006556 S-adenosylmethionine biosynthetic process
GO:0006730 one-carbon metabolic process
GO:0009693 ethylene biosynthetic process
Cellular Component
GO:0005576 extracellular region
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0009505 plant-type cell wall

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6vcy, PDBe:6vcy, PDBj:6vcy
PDBsum6vcy
PubMed32057875
UniProtP23686|METK1_ARATH S-adenosylmethionine synthase 1 (Gene Name=SAM1)

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