7LOZ: S-adenosylmethionine synthetase

S-adenosylmethionine synthetase. Determined by X-ray diffraction at 2.25 Å resolution. Released 31 Mar 2021.

Method
X-ray diffraction
Resolution
2.25 Å
Organism
Escherichia coli 908573
Chains
2
Atoms
6,135
Mol. weight
86.75 kDa
Ligands
POP, PO4, MG
Released
31 Mar 2021

Explore 7LOZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7LOZ contains 35 α-helices and 34 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: 16 helices, 18 β-strands

ElementResiduesLengthSheet
β-strand4-1071
α-helix15-3319
β-strand38-4692
β-strand49-5792
α-helix64-7512
β-strand78-7923
α-helix80-823
β-strand84-8523
β-strand90-9672
α-helix111-1133
α-helix114-1152
β-strand11614
β-strand120-12785
α-helix136-15318
β-strand160-173141
β-strand176-189141
α-helix195-2028
α-helix203-2075
α-helix213-2153
β-strand221-22441
α-helix234-2363
β-strand240-24122
β-strand26512
α-helix270-28718
β-strand29116
β-strand293-30085
β-strand30214
β-strand309-31355
β-strand31816
α-helix322-33211
α-helix337-3448
α-helix352-3554
α-helix366-3683
α-helix373-3797
Chain B: 19 helices, 16 β-strands
ElementResiduesLengthSheet
α-helix-6--52
β-strand3-1087
α-helix15-3319
β-strand38-4698
β-strand49-5798
α-helix64-7512
β-strand78-7929
α-helix80-823
β-strand84-8529
β-strand90-9678
α-helix100-1023
α-helix111-1133
α-helix114-1152
β-strand116110
β-strand120-127811
α-helix136-15318
β-strand160-173147
β-strand176-189147
α-helix195-2028
α-helix203-2075
α-helix213-2153
β-strand221-22447
α-helix234-2363
β-strand240-24128
α-helix246-2494
β-strand26518
α-helix270-28718
β-strand293-300811
β-strand302110
β-strand309-313511
α-helix322-33211
α-helix337-3448
α-helix352-3554
α-helix366-3683
α-helix373-3808

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
S-adenosylmethionine synthaseA, Bprotein392Escherichia coli 908573P0A817 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>7LOZ_1 S-adenosylmethionine synthase (chains A, B)
GLVPRGSHMAKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMVL
VGGEITTSAWVDIEEITRNTVREIGYVHSDMGFDANSCAVLSAIGKQSPDINQGVDRADP
LEQGAGDQGLMFGYATNETDVLMPAPITYAHRLVQRQAEVRKNGTLPWLRPDAKSQVTFQ
YDDGKIVGIDAVVLSTQHSEEIDQKSLQEAVMEEIIKPILPAEWLTSATKFFINPTGRFV
IGGPMGDCGLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLA
DRCEIQVSYAIGVAEPTSIMVETFGTEKVPSEQLTLLVREFFDLRPYGLIQMLDLLHPIY
KETAAYGHFGREHFPWEKTDKAQLLRDAAGLK

Ligands and cofactors

IDNameFormulaCopies
POPPyrophosphate 2-H2 O7 P22
PO4Phosphate ionO4 P4
MGMagnesium ionMg4

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

Primary citation

Substrate Dynamics Contribute to Enzymatic Specificity in Human and Bacterial Methionine Adenosyltransferases. Gade, M., Tan, L.L., Damry, A.M. et al. JACS Au (2021) 1:2349-2360. DOI 10.1021/jacsau.1c00464 · PubMed

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

Browse structure collections

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