1FNM: Thermus thermophilus ef-G H573A

Structure of thermus thermophilus ef-G H573A. Determined by X-ray diffraction at 2.8 Å resolution. Released 22 Nov 2000.

Method
X-ray diffraction
Resolution
2.8 Å
Organism
Thermus thermophilus
Chains
1
Atoms
5,173
Mol. weight
77.38 kDa
Ligands
GDP, MG
Released
22 Nov 2000

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

Secondary structure: helices and β-sheets

1FNM contains 25 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: 25 helices, 42 β-strands

ElementResiduesLengthSheet
α-helix9-113
β-strand12-1541
β-strand17-1932
α-helix25-3612
β-strand69-7461
β-strand77-8261
α-helix91-10010
β-strand104-10962
β-strand11312
α-helix116-12712
β-strand132-13762
α-helix146-1527
α-helix153-1575
β-strand161-16332
β-strand165-16843
β-strand176-17943
β-strand184-18853
β-strand196-19723
α-helix199-2024
α-helix203-22119
α-helix225-2339
α-helix239-25113
β-strand256-26052
β-strand26214
β-strand26714
α-helix269-27911
α-helix287-2882
β-strand289-29245
β-strand298-30145
β-strand310-319101
β-strand323-332101
β-strand334-33636
β-strand339-34351
β-strand348-358111
β-strand363-36641
β-strand368-37036
β-strand374-37961
β-strand388-39031
β-strand39815
β-strand409-41577
α-helix419-43416
β-strand439-44247
β-strand449-45357
α-helix456-46712
β-strand474-47637
α-helix477-4793
β-strand480-48127
β-strand484-48638
β-strand491-49999
β-strand506-516119
α-helix517-5182
β-strand523-52759
α-helix536-5383
α-helix539-54911
α-helix558-5592
β-strand56018
β-strand563-57199
α-helix579-59618
β-strand600-613148
α-helix618-6269
β-strand630-63788
β-strand640-64898
α-helix649-6513
α-helix655-6628
β-strand668-678118
α-helix679-6802
α-helix681-6877

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Elongation factor GAprotein691Thermus thermophilusP13551 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1FNM_1 ELONGATION FACTOR G (chains A)
MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERE
RGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSET
VWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDV
LRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEE
ELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVE
IHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHA
NHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKAD
QEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQ
VAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIP
AVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYAEVDSSEMAFKIAGSMAIKEAVQKGDPV
ILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLR
SKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ

Ligands and cofactors

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

Primary citation

Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site. Laurberg, M., Kristensen, O., Martemyanov, K. et al. J Mol Biol (2000) 303:593-603. DOI 10.1006/jmbi.2000.4168 · 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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