3VH1: Saccharomyces cerevisiae Atg7

Crystal structure of Saccharomyces cerevisiae Atg7 (1-595). Determined by X-ray diffraction at 3.0 Å resolution. Released 21 Sept 2011.

Method
X-ray diffraction
Resolution
3.0 Å
Organism
Saccharomyces cerevisiae
Chains
1
Atoms
4,540
Mol. weight
67.88 kDa
Ligands
ZN
Released
21 Sept 2011

Explore 3VH1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3VH1 contains 24 α-helices and 35 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: 24 helices, 35 β-strands

ElementResiduesLengthSheet
β-strand5-621
α-helix7-82
β-strand1012
β-strand13-1753
α-helix19-3012
β-strand39-4684
β-strand5715
β-strand58-6253
β-strand78-87104
α-helix90-945
α-helix98-11316
α-helix117-1193
β-strand123-13084
β-strand135-146124
β-strand153-15861
α-helix162-17413
β-strand180-18341
β-strand189-19131
α-helix194-2007
β-strand202-20651
β-strand20915
β-strand21612
α-helix219-22911
β-strand235-24171
β-strand248-25471
β-strand269-27354
α-helix274-2763
β-strand284-28744
α-helix289-2924
α-helix294-31320
α-helix319-3235
α-helix3251
β-strand326-33056
α-helix334-34411
β-strand350-35456
β-strand35817
β-strand37817
α-helix379-39012
β-strand395-39956
α-helix403-4053
α-helix413-42917
β-strand432-43546
β-strand43918
α-helix440-4423
α-helix444-4529
β-strand456-46276
β-strand466-47276
β-strand48319
β-strand50518
α-helix513-53018
α-helix532-5343
β-strand539-540210
β-strand543-544210
β-strand548-55256
β-strand557-56156
β-strand56419
α-helix565-5662
α-helix574-58310
α-helix585-5939

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin-like modifier-activating enzyme ATG7Aprotein598Saccharomyces cerevisiaeP38862 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3VH1_1 Ubiquitin-like modifier-activating enzyme ATG7 (chains A)
GPHMSSERVLSYAPAFKSFLDTSFFQELSRLKLDVLKLDSTCQPLTVNLDLHNIPKSADQ
VPLFLTNRSFEKHNNKRTNEVPLQGSIFNFNVLDEFKNLDKQLFLHQRALECWEDGIKDI
NKCVSFVIISFADLKKYRFYYWLGVPCFQRPSSTVLHVRPEPSLKGLFSKCQKWFDVNYS
KWVCILDADDEIVNYDKCIIRKTKVLAIRDTSTMENVPSALTKNFLSVLQYDVPDLIDFK
LLIIRQNEGSFALNATFASIDPQSSSSNPDMKVSGWERNVQGKLAPRVVDLSSLLDPLKI
ADQSVDLNLKLMKWRILPDLNLDIIKNTKVLLLGAGTLGCYVSRALIAWGVRKITFVDNG
TVSYSNPVRQALYNFEDCGKPKAELAAASLKRIFPLMDATGVKLSIPMIGHKLVNEEAQH
KDFDRLRALIKEHDIIFLLVDSRESRWLPSLLSNIENKTVINAALGFDSYLVMRHGNRDE
QSSKQLGCYFCHDVVAPTDSLTDRTLDQMCTVTRPGVAMMASSLAVELMTSLLQTKYSGS
ETTVLGDIPHQIRGFLHNFSILKLETPAYEHCPACSPKVIEAFTDLGWEFVKKALEHP

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2

Primary citation

Structural basis of Atg8 activation by a homodimeric E1, Atg7. Noda, N.N., Satoo, K., Fujioka, Y. et al. Mol Cell (2011) 44:462-475. DOI 10.1016/j.molcel.2011.08.035 · PubMed

Other PDB entries of the same protein (UniProt P38862 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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