2LQ7: NEDD8-activating enzyme E1 catalytic subunit

E2 binding surface on Uba3 beta-grasp domain undergoes a conformational transition. Determined by solution NMR. Released 25 Jul 2012.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
749
Mol. weight
10.66 kDa
Released
25 Jul 2012

Explore 2LQ7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2LQ7 contains 3 α-helices and 7 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: 3 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix3501
β-strand351-35551
β-strand36012
α-helix361-3688
β-strand380-38561
β-strand388-39141
α-helix406-4094
β-strand41112
β-strand421-42661
β-strand433-44081

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
NEDD8-activating enzyme E1 catalytic subunitAprotein97Homo sapiensQ8TBC4 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2LQ7_1 NEDD8-activating enzyme E1 catalytic subunit (chains A)
GSQLPQNIQFSPSAKLQEVLDYLTNSASLQMKSPAITATLEGKNRTLYLQSVTSIEERTR
PNLSKTLKELGLVDGQELAVADVTTPQTVLFKLHFTS

Primary citation

E2-binding surface on Uba3 beta-grasp domain undergoes a conformational transition. Elgin, E.S., Sokmen, N., Peterson, F.C. et al. Proteins (2012) 80:2482-2487. DOI 10.1002/prot.24148 · 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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