2CYX: Human ubiquitin-conjugating enzyme E2 G2

Structure of human ubiquitin-conjugating enzyme E2 G2 (UBE2G2/UBC7). Determined by X-ray diffraction at 2.56 Å resolution. Released 25 Apr 2006.

Method
X-ray diffraction
Resolution
2.56 Å
Organism
Homo sapiens
Chains
3
Atoms
4,019
Mol. weight
57.18 kDa
Released
25 Apr 2006

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

Secondary structure: helices and β-sheets

2CYX contains 25 α-helices and 21 β-strands across 3 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: 9 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix-1-1819
α-helix20-212
β-strand24-2851
β-strand36-4271
β-strand53-5971
α-helix68-692
β-strand70-7341
β-strand8212
β-strand8711
β-strand8812
α-helix91-933
α-helix105-1084
α-helix116-12813
α-helix135-1373
α-helix138-1458
α-helix148-16215
Chain B: 7 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix-1-1819
α-helix20-212
β-strand24-2853
β-strand36-4273
α-helix43-442
β-strand53-5973
β-strand70-7343
β-strand8214
β-strand8713
β-strand8814
α-helix91-933
α-helix116-12813
α-helix138-1458
α-helix148-16215
Chain C: 9 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix-1-1819
α-helix20-212
β-strand24-2855
β-strand36-4275
α-helix43-442
β-strand53-5975
β-strand70-7345
β-strand8216
β-strand8715
β-strand8816
α-helix91-933
α-helix105-1084
α-helix116-12813
α-helix135-1373
α-helix138-1458
α-helix148-16215

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin-conjugating enzyme E2 G2A, B, Cprotein170Homo sapiensP60604 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>2CYX_1 Ubiquitin-conjugating enzyme E2 G2 (chains A, B, C)
GGSEFMAGTALKRLMAEYKQLTLNPPEGIVAGPMNEENFFEWEALIMGPEDTCFEFGVFP
AILSFPLDYPLSPPKMRFTCEMFHPNIYPDGRVCISILHAPGDDPMGYESSAERWSPVQS
VEKILLSVVSMLAEPNDESGANVDASKMWRDDREQFYKIAKQIVQKSLGL

Primary citation

Structure of human ubiquitin-conjugating enzyme E2 G2 (UBE2G2/UBC7). Arai, R., Yoshikawa, S., Murayama, K. et al. Acta Crystallogr Sect F Struct Biol Cryst Commun (2006) 62:330-334. DOI 10.1107/S1744309106009006 · PubMed

Other PDB entries of the same protein (UniProt P60604 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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