3IZP: Conformation of EF-G during translocation

Conformation of EF-G during translocation. Determined by electron microscopy. Released 16 Mar 2011.

Method
Electron microscopy
Organism
Thermus thermophilus
Chains
1
Atoms
5,382
Mol. weight
76.6 kDa
Released
16 Mar 2011

Explore 3IZP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3IZP contains 22 α-helices and 41 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 E: 22 helices, 41 β-strands

ElementResiduesLengthSheet
α-helix4-107
β-strand15-1951
α-helix24-3714
α-helix55-606
β-strand6211
β-strand70-7452
β-strand77-8152
α-helix91-10010
β-strand103-10971
α-helix116-12712
β-strand132-13761
α-helix146-15611
β-strand161-16331
β-strand166-16833
β-strand176-17943
β-strand184-18853
β-strand196-19723
α-helix1991
β-strand20013
α-helix201-2022
α-helix203-22119
α-helix225-2339
α-helix239-25113
β-strand256-26051
α-helix269-27911
β-strand289-29244
β-strand298-30144
β-strand310-31895
β-strand324-33295
β-strand335-33626
β-strand339-34355
β-strand348-358115
β-strand363-36645
β-strand368-36926
β-strand374-37965
β-strand388-39035
β-strand409-41357
β-strand414-41528
α-helix419-43416
β-strand438-43927
β-strand442-44327
β-strand448-45367
α-helix456-46510
α-helix466-4705
β-strand474-47528
β-strand484-48639
β-strand491-5001010
β-strand505-5161210
β-strand523-527510
α-helix536-5383
α-helix539-54911
β-strand56019
β-strand563-570810
β-strand577110
α-helix579-59618
β-strand600-612139
α-helix617-62610
β-strand631-63779
β-strand640-64899
α-helix649-6513
α-helix656-6627
β-strand668-678119
α-helix681-6844

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Elongation factor GEprotein688Thermus thermophilusP13551 (AlphaFold model)
Sequence of entity 1 (E), FASTA
>3IZP_1 Elongation factor G (chains E)
MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERE
RGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSET
VWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDV
LRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEE
ELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVE
IHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHA
NHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKAD
QEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQ
VAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIP
AVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYAEVDSSEMAFKIAGSMAIKEAVQKGDPV
ILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLR
SKTQGRGSFVMFFDHYQEVPKQVQEKLI

Primary citation

Molecular dynamics of EF-G during translocation. Li, W., Trabuco, L.G., Schulten, K. et al. Proteins (2011) 79:1478-1486. DOI 10.1002/prot.22976 · PubMed

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

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