2NPF: EEF2

Structure of eEF2 in complex with moriniafungin. Determined by X-ray diffraction at 2.9 Å resolution. Released 14 Nov 2006.

Method
X-ray diffraction
Resolution
2.9 Å
Organism
Saccharomyces cerevisiae
Chains
2
Atoms
12,885
Mol. weight
189.08 kDa
Ligands
GDP, MOU
Released
14 Nov 2006

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

Secondary structure: helices and β-sheets

2NPF contains 80 α-helices and 97 β-strands across 2 chains. 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: 41 helices, 49 β-strands

ElementResiduesLengthSheet
β-strand411
α-helix6-149
α-helix16-183
β-strand19-2682
α-helix32-4312
β-strand4412
β-strand4711
β-strand7013
β-strand74-8072
α-helix85-873
β-strand97-10372
α-helix112-1198
β-strand124-13072
β-strand13412
α-helix137-14812
β-strand152-15872
α-helix160-1612
α-helix162-1665
α-helix171-19222
β-strand209-21352
β-strand218-22032
α-helix222-2287
α-helix237-2437
β-strand249-25134
β-strand256-25834
β-strand26215
β-strand26815
β-strand27114
α-helix2721
α-helix273-2786
α-helix279-28911
α-helix295-3039
α-helix309-3135
α-helix316-32712
β-strand32912
α-helix330-34112
α-helix343-3442
α-helix345-35612
β-strand35716
α-helix364-3718
β-strand379-38797
β-strand38813
β-strand394-40297
β-strand404-40638
β-strand410-41457
β-strand41919
β-strand42219
β-strand428-43037
β-strand433-43867
β-strand441-44557
β-strand447-44938
β-strand453-45757
β-strand467-47047
β-strand47816
α-helix481-4833
β-strand489-495710
α-helix498-5003
α-helix501-51414
β-strand519-522410
β-strand528-532510
α-helix535-54410
α-helix545-5495
β-strand554-557410
α-helix558-5625
β-strand564-567411
β-strand575-578412
β-strand585-592812
α-helix593-5942
α-helix595-6028
α-helix612-6176
α-helix618-6225
β-strand633-636412
β-strand644-647412
α-helix655-6573
α-helix660-67213
α-helix679-6802
β-strand681111
β-strand684-692912
α-helix697-6993
α-helix702-71817
β-strand722-7351411
α-helix740-7489
β-strand753-758611
β-strand766-773811
α-helix774-7763
α-helix780-7867
β-strand793111
β-strand796-804911
α-helix814-82613
α-helix835-8373
Chain B: 39 helices, 48 β-strands
ElementResiduesLengthSheet
β-strand4113
α-helix6-127
α-helix16-183
β-strand19-25714
α-helix32-4312
β-strand44114
β-strand47113
β-strand69115
β-strand70116
β-strand74-80714
α-helix85-873
β-strand97-103714
α-helix112-1198
β-strand124-130714
β-strand134114
α-helix137-14812
β-strand152-158714
α-helix160-1656
α-helix171-19222
β-strand209-213514
β-strand218-220314
α-helix222-23110
α-helix237-2437
β-strand249-251317
β-strand256-258317
β-strand262118
β-strand268118
β-strand271117
α-helix272-2732
α-helix274-2785
α-helix279-28911
α-helix295-3028
α-helix309-3113
α-helix317-32711
β-strand329114
α-helix330-34112
α-helix343-3442
α-helix345-35612
β-strand357119
α-helix364-3718
β-strand379-387915
β-strand388116
β-strand394-402915
β-strand404-406320
β-strand410-414515
β-strand426-430515
β-strand433-438615
β-strand441-445515
β-strand447-449320
β-strand452-457615
β-strand467-470415
β-strand478119
β-strand489-495721
α-helix498-5003
α-helix501-51414
β-strand519-522421
β-strand528-532521
α-helix535-54410
α-helix545-5495
β-strand554-557421
α-helix558-5625
β-strand564-567422
β-strand575-578423
β-strand585-592823
α-helix593-5942
α-helix595-6028
α-helix612-6176
α-helix618-6225
α-helix630-6323
β-strand633-636423
β-strand644-648523
α-helix660-67213
α-helix679-6802
β-strand681122
β-strand684-692923
α-helix697-6993
α-helix702-71817
β-strand722-7351422
α-helix740-74910
β-strand753-758622
β-strand766-773822
α-helix774-7763
α-helix780-7867
β-strand793122
β-strand796-804922
α-helix814-82613
α-helix835-8373

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Elongation factor 2A, Bprotein842Saccharomyces cerevisiaeP32324 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2NPF_1 Elongation factor 2 (chains A, B)
MVAFTVDQMRSLMDKVTNVRNMSVIAHVDHGKSTLTDSLVQRAGIISAAKAGEARFTDTR
KDEQERGITIKSTAISLYSEMSDEDVKEIKQKTDGNSFLINLIDSPGHVDFSSEVTAALR
VTDGALVVVDTIEGVCVQTETVLRQALGERIKPVVVINKVDRALLELQVSKEDLYQTFAR
TVESVNVIVSTYADEVLGDVQVYPARGTVAFGSGLHGWAFTIRQFATRYAKKFGVDKAKM
MDRLWGDSFFNPKTKKWTNKDTDAEGKPLERAFNMFILDPIFRLFTAIMNFKKDEIPVLL
EKLEIVLKGDEKDLEGKALLKVVMRKFLPAADALLEMIVLHLPSPVTAQAYRAEQLYEGP
ADDANCIAIKNCDPKADLMLYVSKMVPTSDKGRFYAFGRVFAGTVKSGQKVRIQGPNYVP
GKKDDLFIKAIQRVVLMMGRFVEPIDDCPAGNIIGLVGIDQFLLKTGTLTTSETAHNMKV
MKFSVSPVVQVAVEVKNANDLPKLVEGLKRLSKSDPCVLTYMSESGEHIVAGTGELHLEI
CLQDLEHDHAGVPLKISPPVVAYRETVESESSQTALSKSPNKHNRIYLKAEPIDEEVSLA
IENGIINPRDDFKARARIMADDYGWDVTDARKIWCFGPDGNGPNLVIDQTKAVQYLHEIK
DSVVAAFQWATKEGPIFGEEMRSVRVNILDVTLHADAIHRGGGQIIPTMRRATYAGFLLA
DPKIQEPVFLVEIQCPEQAVGGIYSVLNKKRGQVVSEEQRPGTPLFTVKAYLPVNESFGF
TGELRQATGGQAFPQMVFDHWSTLGSDPLDPTSKAGEIVLAARKRHGMKEEVPGWQEYYD
KL

Ligands and cofactors

IDNameFormulaCopies
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P22
MOU(1S,4R,5R,9S,11S)-2-({[(2S,5R,6R,7R,9S,10R)-2-(7-carboxyheptyl)-6-hydroxy-10-me…C37 H54 O122

Primary citation

Sordarin derivatives induce a novel conformation of the yeast ribosome translocation factor eEF2. Soe, R., Mosley, R.T., Justice, M. et al. J Biol Chem (2007) 282:657-666. DOI 10.1074/jbc.M607830200 · 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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