2BM1: Elongation factor G

Ribosomal elongation factor G (EF-G) Fusidic acid resistant mutant G16V. Determined by X-ray diffraction at 2.6 Å resolution. Released 4 May 2005.

Method
X-ray diffraction
Resolution
2.6 Å
Organism
THERMUS THERMOPHILUS
Chains
1
Atoms
5,258
Mol. weight
77.49 kDa
Ligands
MG, GDP
Released
4 May 2005

Explore 2BM1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2BM1 contains 30 α-helices and 46 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: 30 helices, 46 β-strands

ElementResiduesLengthSheet
α-helix9-113
β-strand12-1981
α-helix25-3713
β-strand69-7461
β-strand77-8261
α-helix831
α-helix93-1008
β-strand103-10971
β-strand11311
α-helix118-12710
β-strand132-13761
α-helix146-15712
β-strand161-16331
β-strand165-16842
α-helix171-1733
β-strand176-17942
β-strand184-18852
β-strand196-19942
α-helix200-2023
α-helix203-2053
α-helix206-22116
α-helix225-2317
α-helix236-2383
α-helix239-25113
β-strand256-26051
β-strand26213
β-strand26713
α-helix269-27911
α-helix281-2822
α-helix283-2853
α-helix287-2893
β-strand290-29234
β-strand298-30034
β-strand310-31781
β-strand325-33281
β-strand334-33635
β-strand340-34341
β-strand348-358111
β-strand363-36531
β-strand368-37035
β-strand374-37961
β-strand388-39031
β-strand39814
β-strand409-41136
β-strand412-41327
β-strand41418
α-helix425-4273
α-helix431-4333
β-strand439-44137
β-strand449-45247
β-strand45316
α-helix456-4605
α-helix463-4653
β-strand47518
β-strand479-48136
β-strand484-48639
β-strand491-5001010
β-strand505-5161210
α-helix517-5182
β-strand523-527510
α-helix539-55012
β-strand56019
β-strand563-571910
β-strand577110
α-helix579-59618
β-strand600-613149
α-helix614-6163
α-helix617-6237
α-helix625-6273
β-strand631-63779
β-strand640-64899
α-helix649-6524
α-helix656-6594
β-strand66819
β-strand672-67879
α-helix681-6866

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Elongation factor GAprotein691THERMUS THERMOPHILUSP13551 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2BM1_1 ELONGATION FACTOR G (chains A)
MAVKVEYDLKRLRNIVIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERE
RGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSET
VWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDV
LRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEE
ELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVE
IHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHA
NHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKAD
QEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQ
VAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIP
AVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPV
ILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLR
SKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P21

Primary citation

Structural Insights Into Fusidic Acid Resistance and Sensitivity in EF-G. Hansson, S., Singh, R., Gudkov, A.T. et al. J Mol Biol (2005) 348:939. DOI 10.1016/J.JMB.2005.02.066 · PubMed

Other PDB entries of the same protein (UniProt P13551 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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