1MXA: S-adenosylmethionine synthetase with ppi

S-adenosylmethionine synthetase with ppi. Determined by X-ray diffraction at 2.8 Å resolution. Released 11 Jul 1996.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Escherichia coli
Chains: 1
Atoms: 2,917
Mol. weight: 42.27 kDa
Ligands: POP, MG, PO4
Released: 11 Jul 1996

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

Secondary structure: helices and β-sheets

1MXA 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	15-31	17
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	160-172	13	1
β-strand	177-189	13	1
α-helix	195-202	8
α-helix	203-207	5
α-helix	213-215	3
β-strand	221-224	4	1
β-strand	239-241	3	2
α-helix	246-250	5
β-strand	265	1	2
α-helix	270-287	18
β-strand	293-300	8	4
β-strand	309-314	6	4
α-helix	322-332	11
α-helix	337-343	7
α-helix	352-355	4
α-helix	366-368	3
α-helix	373-379	7

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

>1MXA_1 S-ADENOSYLMETHIONINE SYNTHETASE (chains A)
AKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMVLVGGEITTSA
WVDIEEITRNTVREIGYVHSDMGFDANSCAVLSAIGKQSPDINQGVDRADPLEQGAGDQG
LMFGYATNETDVLMPAPITYAHRLVQRQAEVRKNGTLPWLRPDAKSQVTFQYDDGKIVGI
DAVVLSTQHSEEIDQKSLQEAVMEEIIKPILPAEWLTSATKFFINPTGRFVIGGPMGDCG
LTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQVSY
AIGVAEPTSIMVETFGTEKVPSEQLTLLVREFFDLRPYGLIQMLDLLHPIYKETAAYGHF
GREHFPWEKTDKAQLLRDAAGLK

Ligands and cofactors

ID	Name	Formula	Copies
POP	Pyrophosphate 2-	H2 O7 P2	1
MG	Magnesium ion	Mg	2
PO4	Phosphate ion	O4 P	1

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

Primary citation

Structure and function of S-adenosylmethionine synthetase: crystal structures of S-adenosylmethionine synthetase with ADP, BrADP, and PPi at 28 angstroms resolution. Takusagawa, F., Kamitori, S., Markham, G.D. Biochemistry (1996) 35:2586-2596. DOI 10.1021/bi952604z · 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…
1MXB 2.8 Å, S-adenosylmethionine synthetase with ADP
8BB1 2.8 Å, T3 SAM lyase in complex with S-adenosylmethionine synthase
1MXC 3.0 Å, S-adenosylmethionine synthetase with 8-br-ADP

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