1U2R: Elongation factor 2

Crystal Structure of ADP-ribosylated Ribosomal Translocase from Saccharomyces cerevisiae. Determined by X-ray diffraction at 2.6 Å resolution. Released 14 Sept 2004.

Method
X-ray diffraction
Resolution
2.6 Å
Organism
Saccharomyces cerevisiae
Chains
1
Atoms
6,670
Mol. weight
95.07 kDa
Ligands
MG, APR, SO1, GDP
Released
14 Sept 2004

Explore 1U2R in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1U2R contains 44 α-helices and 47 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: 44 helices, 47 β-strands

ElementResiduesLengthSheet
β-strand411
α-helix6-127
α-helix16-183
β-strand19-2682
α-helix32-4312
β-strand4412
β-strand4711
β-strand7013
β-strand74-8072
α-helix83-886
β-strand97-10372
α-helix113-1208
β-strand124-13072
β-strand13412
α-helix137-14711
α-helix1511
β-strand152-15872
α-helix160-1656
α-helix171-19222
α-helix195-1973
α-helix204-2063
β-strand209-21352
β-strand218-22142
α-helix222-23312
α-helix237-2437
β-strand249-25134
β-strand256-25834
β-strand26215
β-strand26815
β-strand27114
α-helix272-2732
α-helix274-2785
α-helix279-28911
α-helix296-3027
α-helix309-3135
α-helix316-32712
β-strand32912
α-helix330-34112
α-helix343-3442
α-helix345-35612
β-strand35716
α-helix364-3707
β-strand379-38797
β-strand38813
β-strand394-40297
β-strand404-40638
β-strand410-41457
β-strand426-43057
β-strand433-43867
β-strand441-44557
β-strand447-44938
β-strand453-45757
β-strand467-47047
α-helix476-4772
β-strand47816
α-helix480-4823
β-strand489-49579
α-helix498-5003
α-helix501-51414
β-strand519-52249
β-strand528-53259
α-helix535-54410
α-helix545-5495
β-strand554-55749
α-helix558-5625
β-strand564-567410
β-strand575-578411
β-strand585-592811
α-helix593-5942
α-helix595-6039
α-helix612-62110
α-helix627-6315
β-strand633-636411
β-strand644-648511
α-helix656-67217
α-helix6791
β-strand680-681210
β-strand684-692911
α-helix697-6993
α-helix702-71817
β-strand722-7351410
α-helix737-74913
β-strand753-758610
β-strand766-773810
α-helix774-7763
α-helix780-7878
β-strand793110
β-strand796-803810
α-helix814-82512
α-helix832-8343
α-helix835-8384

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Elongation factor 2Aprotein842Saccharomyces cerevisiaeP32324 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1U2R_1 Elongation factor 2 (chains A)
MVAFTVDQMRSLMDKVTNVRNMSVIAHVDHGKSTLTDSLVQRAGIISAAKAGEARFTDTR
KDEQERGITIKSTAISLYSEMSDEDVKEIKQKTDGNSFLINLIDSPGHVDFSSEVTAALR
VTDGALVVVDTIEGVCVQTETVLRQALGERIKPVVVINKVDRALLELQVSKEDLYQTFAR
TVESVNVIVSTYADEVLGDVQVYPARGTVAFGSGLHGWAFTIRQFATRYAKKFGVDKAKM
MDRLWGDSFFNPKTKKWTNKDTDAEGKPLERAFNMFILDPIFRLFTAIMNFKKDEIPVLL
EKLEIVLKGDEKDLEGKALLKVVMRKFLPAADALLEMIVLHLPSPVTAQAYRAEQLYEGP
ADDANCIAIKNCDPKADLMLYVSKMVPTSDKGRFYAFGRVFAGTVKSGQKVRIQGPNYVP
GKKDDLFIKAIQRVVLMMGRFVEPIDDCPAGNIIGLVGIDQFLLKTGTLTTSETAHNMKV
MKFSVSPVVQVAVEVKNANDLPKLVEGLKRLSKSDPCVLTYMSESGEHIVAGTGELHLEI
CLQDLEHDHAGVPLKISPPVVAYRETVESESSQTALSKSPNKHNRIYLKAEPIDEEVSLA
IENGIINPRDDFKARARIMADDYGWDVTDARKIWCFGPDGNGPNLVIDQTKAVQYLHEIK
DSVVAAFQWATKEGPIFGEEMRSVRVNILDVTLHADAIHRGGGQIIPTMRRATYAGFLLA
DPKIQEPVFLVEIQCPEQAVGGIYSVLNKKRGQVVSEEQRPGTPLFTVKAYLPVNESFGF
TGELRQATGGQAFPQMVFDHWSTLGSDPLDPTSKAGEIVLAARKRHGMKEEVPGWQEYYD
KL

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1
APRAdenosine-5-diphosphoriboseC15 H23 N5 O14 P21
SO1[1R-(1.ALPHA.,3A.BETA.,4.BETA.,4A.BETA.,7.BETA.,7A.ALPHA.,8A.BETA.)]8A-[(6-deox…C27 H42 O81
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P21

Primary citation

Crystal Structure of ADP-ribosylated Ribosomal Translocase from Saccharomyces cerevisiae. Jorgensen, R., Yates, S.P., Teal, D.J. et al. J Biol Chem (2004) 279:45919-45925. DOI 10.1074/jbc.M406218200 · PubMed

Other PDB entries of the same protein (UniProt P32324 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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