1FUG: S-adenosylmethionine synthetase

S-adenosylmethionine synthetase. Determined by X-ray diffraction at 3.2 Å resolution. Released 1 Aug 1996.

Method: X-ray diffraction
Resolution: 3.2 Å
Organism: Escherichia coli
Chains: 2
Atoms: 5,884
Mol. weight: 83.73 kDa
Released: 1 Aug 1996

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

Secondary structure: helices and β-sheets

1FUG contains 27 α-helices and 36 β-strands across 2 chains. 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: 11 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	4-10	7	1
β-strand	12	1	2
β-strand	14	1	2
α-helix	15-32	18
β-strand	43-46	4	3
β-strand	49-56	8	3
α-helix	64-75	12
β-strand	90-97	8	3
β-strand	120-127	8	4
α-helix	136-151	16
β-strand	165-171	7	1
β-strand	174	1	5
β-strand	176	1	5
β-strand	179-186	8	1
α-helix	195-201	7
α-helix	202-207	6
β-strand	221-224	4	1
α-helix	234-236	3
β-strand	239-241	3	3
β-strand	256	1	6
β-strand	258	1	4
α-helix	270-287	18
β-strand	291	1	7
β-strand	293-300	8	4
β-strand	309	1	4
β-strand	313	1	4
β-strand	318	1	7
α-helix	322-332	11
α-helix	337-342	6
α-helix	352-356	5
α-helix	374-380	7

Chain B: 16 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	3-4	2	8
β-strand	7-10	4	8
α-helix	15-33	19
β-strand	39-46	8	9
β-strand	49-57	9	9
α-helix	64-74	11
α-helix	80-82	3
β-strand	90-98	9	9
α-helix	112-114	3
β-strand	120-125	6	10
α-helix	137-144	8
α-helix	147-154	8
β-strand	160-172	13	8
β-strand	179-189	11	8
α-helix	195-201	7
α-helix	202-207	6
α-helix	213-215	3
β-strand	221	1	8
β-strand	224	1	8
α-helix	247-250	4
β-strand	256	1	6
β-strand	265	1	9
α-helix	270-287	18
β-strand	291	1	11
β-strand	294-300	7	10
β-strand	311-314	4	10
β-strand	318	1	11
α-helix	325-332	8
α-helix	337-343	7
α-helix	352-357	6
α-helix	366-368	3
α-helix	374-377	4

Molecules and chains

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

Sequence of entity 1 (A, B), FASTA

>1FUG_1 S-ADENOSYLMETHIONINE SYNTHETASE (chains A, B)
AKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMVLVGGEITTSA
WVDIEEITRNTVREIGYVHSDMGFDANSCAVLSAIGKQSPDINQGVDRADPLEQGAGDQG
LMFGYATNETDVLMPAPITYAHRLVQRQAEVRKNGTLPWLRPDAKSQVTFQYDDGKIVGI
DAVVLSTQHSEEIDQKSLQEAVMEEIIKPILPAEWLTSATKFFINPTGRFVIGGPMGDCG
LTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQVSY
AIGVAEPTSIMVETFGTEKVPSEQLTLLVREFFDLRPYGLIQMLDLLHPIYKETAAYGHF
GREHFPWEKTDKAQLLRDAAGLK

Primary citation

Flexible loop in the structure of S-adenosylmethionine synthetase crystallized in the tetragonal modification. Fu, Z., Hu, Y., Markham, G.D. et al. J Biomol Struct Dyn (1996) 13:727-739. 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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