1XRC: S-adenosylmethionine synthetase

Crystal structure of S-adenosylmethionine synthetase. Determined by X-ray diffraction at 3.0 Å resolution. Released 8 Mar 1996.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Escherichia coli
Chains: 1
Atoms: 2,912
Mol. weight: 42.25 kDa
Ligands: CO, PO4
Released: 8 Mar 1996

Explore 1XRC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1XRC contains 16 α-helices and 14 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 16 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	3-10	8	1
α-helix	15-33	19
β-strand	38-46	9	2
β-strand	49-57	9	2
α-helix	64-75	12
β-strand	78-79	2	3
α-helix	80-82	3
β-strand	84-85	2	3
β-strand	90-98	9	2
α-helix	111-113	3
α-helix	114-116	3
β-strand	120-127	8	4
α-helix	136-153	18
β-strand	160-173	14	1
β-strand	176-189	14	1
α-helix	195-202	8
α-helix	203-207	5
α-helix	213-215	3
β-strand	221-224	4	1
β-strand	240-241	2	2
α-helix	246-249	4
β-strand	265	1	2
α-helix	270-287	18
β-strand	293-300	8	4
β-strand	309-313	5	4
α-helix	322-332	11
α-helix	337-343	7
α-helix	352-355	4
α-helix	366-368	3
α-helix	373-377	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
S-adenosylmethionine synthetase	A	protein	383	Escherichia coli	P0A817 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1XRC_1 S-ADENOSYLMETHIONINE SYNTHETASE (chains A)
AKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMVLVGGEITTSA
WVDIEEITRNTVREIGYVHSDMGFDANSCAVLSAIGKQSPDINQGVDRADPLEQGAGDQG
LMFGYATNETDVLMPAPITYAHRLVQRQAEVRKNGTLPWLRPDAKSQVTFQYDDGKIVGI
DAVVLSTQHSEEIDQKSLQEAVMEEIIKPILPAEWLTSATKFFINPTGRFVIGGPMGDCG
LTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQVSY
AIGVAEPTSIMVETFGTEKVPSEQLTLLVREFFDLRPYGLIQMLDLLHPIYKETAAYGHF
GREHFPWEKTDKAQLLRDAAGLK

Ligands and cofactors

ID	Name	Formula	Copies
CO	Cobalt (II) ion	Co	2
PO4	Phosphate ion	O4 P	2

Water and common crystallization additives (K) are not listed.

Primary citation

Crystal structure of S-adenosylmethionine synthetase. Takusagawa, F., Kamitori, S., Misaki, S. et al. J Biol Chem (1996) 271:136-147. DOI 10.1074/jbc.271.1.136 · PubMed

Other PDB entries of the same protein (UniProt P0A817 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7R2W 1.6 Å, Mutant S-adenosylmethionine synthetase from E.coli complexed with AMPPNP and methionine
7LO2 1.89 Å, S-adenosylmethionine synthetase cocrystallized with CTP
7LOO 1.95 Å, S-adenosyl methionine transferase cocrystallized with ATP
7LL3 2.24 Å, S-adenosylmethionine synthetase co-crystallized with UppNHp
7LOZ 2.25 Å, S-adenosylmethionine synthetase
7LOW 2.39 Å, S-adenosylmethionine synthetase
1P7L 2.5 Å, S-Adenosylmethionine synthetase complexed with AMPPNP and Met.
1RG9 2.5 Å, S-Adenosylmethionine synthetase complexed with SAM and PPNP
7LNN 2.5 Å, E. coli S-adenosyl methionine transferase co-crystallized with…
1MXA 2.8 Å, S-adenosylmethionine synthetase with ppi
1MXB 2.8 Å, S-adenosylmethionine synthetase with ADP
8BB1 2.8 Å, T3 SAM lyase in complex with S-adenosylmethionine synthase

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