Structure of PDB 2obv Chain A

Receptor sequence

>2obvA (length=384) Species: 9606 (Homo sapiens)

FQSMGVFMFTSESVGEGHPDKICDQISDAVLDAHLKQDPNAKVACETVCK
TGMVLLCGEITSMAMVDYQRVVRDTIKHIGYDDSAKGFDFKTCNVLVALE
QQSPDIAQCVHLDRNEEDVGAGDQGLMFGYATDETEECMPLTIILAHKLN
ARMADLRRSGLLPWLRPDSKTQVTVQYMQDNGAVIPVRIHTIVISVQHNE
DITLEEMRRALKEQVIRAVVPAKYLDEDTVYHLQPSGRFVIGGPQGDAGV
TGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKAGLC
RRVLVQVSYAIGVAEPLSISIFTYGTSQKTERELLDVVHKNFDLRPGVIV
RDLDLKKPIYQKTACYGHFGRSEFPWEVPRKLVF

3D structure

• PDB: 2obv Crystal structure of the human S-adenosylmethionine synthetase 1 in complex with the product.
• Chain: A
• Resolution: 2.05 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H29 D31 K32 E57 E70 K181 F250 D258 A259 R264 K265 K285 K289 D291
• Catalytic site (residue number reindexed from 1): H18 D20 K21 E46 E59 K170 F239 D247 A248 R253 K254 K274 K278 D280
• 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	SAM	A	H29 P30 D179 K181 S247 F250 D258	H18 P19 D168 K170 S236 F239 D247

Gene Ontology

Molecular Function

• GO:0004478 methionine adenosyltransferase activity
• GO:0005515 protein binding
• GO:0005524 ATP binding
• GO:0016740 transferase activity
• 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:0009087 methionine catabolic process
• GO:0051289 protein homotetramerization

Cellular Component

• GO:0005829 cytosol
• GO:0048269 methionine adenosyltransferase complex

External links

• PDB: RCSB:2obv, PDBe:2obv, PDBj:2obv
• PDBsum: 2obv
• UniProt: Q00266|METK1_HUMAN S-adenosylmethionine synthase isoform type-1 (Gene Name=MAT1A)