3FN1: NEDD8-activating enzyme E1 catalytic subunit

E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification. Determined by X-ray diffraction at 2.5 Å resolution. Released 17 Mar 2009.

Method
X-ray diffraction
Resolution
2.5 Å
Organism
Homo sapiens
Chains
2
Atoms
2,127
Mol. weight
29.96 kDa
Released
17 Mar 2009

Explore 3FN1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3FN1 contains 11 α-helices and 17 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: 4 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand351-35551
β-strand36012
α-helix361-37010
β-strand380-38561
β-strand388-39471
α-helix398-4047
α-helix405-4095
β-strand41112
α-helix417-4182
β-strand422-42651
β-strand434-44071
Chain B: 7 helices, 10 β-strands
ElementResiduesLengthSheet
α-helix32-4413
α-helix45-473
β-strand52-5543
β-strand64-6963
β-strand81-8663
β-strand9114
β-strand9414
α-helix95-962
β-strand97-10043
β-strand10915
β-strand11515
α-helix118-1203
β-strand12216
β-strand13016
α-helix136-14510
α-helix159-1679
α-helix169-18315

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
NEDD8-activating enzyme E1 catalytic subunitAprotein98Homo sapiensQ8TBC4 (AlphaFold model)
NEDD8-conjugating enzyme UBE2FBprotein167Homo sapiensQ969M7 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3FN1_1 NEDD8-activating enzyme E1 catalytic subunit (chains A)
GSSQLPQNIQFSPSAKLQEVLDYLTNSASLQMKSPAITATLEGKNRTLYMQSVTSIEERT
RPNLSKTLKELGLVDGQELAVADVTTPQTVLFKLHFTS
Sequence of entity 2 (B), FASTA
>3FN1_2 NEDD8-conjugating enzyme UBE2F (chains B)
GSATASDSTRRVSVRDKLLVKEVAELEANLPCTCKVHFPDPNKLHCFQLTVTPDEGYYQG
GKFQFETEVPDAYNMVPPKVKCLTKIWHPNITETGEICLSLLREHSIDGTGWAPTRTLKD
VVWGLNSLFTDLLNFDDPLNIEAAEHHLRDKEDFRNKVDDYIKRYAR

Primary citation

E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification. Huang, D.T., Ayrault, O., Hunt, H.W. et al. Mol Cell (2009) 33:483-495. DOI 10.1016/j.molcel.2009.01.011 · PubMed

Other PDB entries of the same protein (UniProt Q8TBC4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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