2BM0: Elongation factor G

Ribosomal elongation factor G (EF-G) Fusidic acid resistant mutant T84A. Determined by X-ray diffraction at 2.4 Å resolution. Released 4 May 2005.

Method
X-ray diffraction
Resolution
2.4 Å
Organism
THERMUS THERMOPHILUS
Chains
1
Atoms
5,363
Mol. weight
77.43 kDa
Ligands
MG, GDP
Released
4 May 2005

Explore 2BM0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2BM0 contains 34 α-helices and 42 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: 34 helices, 42 β-strands

ElementResiduesLengthSheet
α-helix9-113
β-strand12-1981
α-helix25-3612
α-helix651
α-helix671
β-strand69-7461
β-strand77-8261
α-helix91-10010
β-strand103-10861
α-helix118-12710
β-strand132-13651
β-strand13812
α-helix146-15510
β-strand161-16331
β-strand165-16843
α-helix171-1733
β-strand176-17943
β-strand184-18853
β-strand196-19943
α-helix200-2012
α-helix203-2053
α-helix206-22015
α-helix221-2233
α-helix225-2339
α-helix235-2384
α-helix239-25113
β-strand256-26051
β-strand26212
β-strand26712
α-helix269-27911
α-helix281-2822
α-helix287-2882
β-strand289-29244
β-strand298-30144
β-strand310-31785
β-strand325-33285
β-strand334-33636
β-strand340-34345
β-strand348-358115
β-strand363-36645
β-strand368-37036
β-strand374-37965
β-strand388-39035
β-strand39814
α-helix401-4022
β-strand409-41577
α-helix419-42911
α-helix431-4344
β-strand439-44247
β-strand449-45357
α-helix456-4649
α-helix465-4695
β-strand474-47637
α-helix477-4793
β-strand480-48127
β-strand484-48638
β-strand491-501119
β-strand504-516139
α-helix517-5182
β-strand523-52759
α-helix536-5383
α-helix539-55012
β-strand56018
β-strand563-57199
β-strand57719
α-helix579-59618
β-strand600-612138
α-helix614-6163
α-helix617-62610
β-strand630-63788
β-strand640-64898
α-helix649-6513
α-helix655-6628
β-strand668-678118
α-helix679-6802
α-helix681-6866

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Elongation factor GAprotein691THERMUS THERMOPHILUSP13551 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2BM0_1 ELONGATION FACTOR G (chains A)
MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIAEVHEGAATMDFMEQERE
RGITITAAVTTCFWKDHRINIIDAPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSET
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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