4GB0: RING domain of RNF168

Crystal Structure of the RING domain of RNF168. Determined by X-ray diffraction at 2.6 Å resolution. Released 10 Jul 2013.

Method
X-ray diffraction
Resolution
2.6 Å
Organism
Homo sapiens
Chains
1
Atoms
743
Mol. weight
14.15 kDa
Ligands
MLI, ZN
Released
10 Jul 2013

Explore 4GB0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4GB0 contains 6 α-helices and 6 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: 6 helices, 6 β-strands

ElementResiduesLengthSheet
α-helix12-143
β-strand1511
β-strand2211
β-strand26-2832
β-strand34-3632
α-helix37-393
α-helix40-489
β-strand5013
β-strand5713
α-helix59-679
α-helix74-8310
α-helix85-928

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligase RNF168Aprotein121Homo sapiensQ8IYW5 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4GB0_1 E3 ubiquitin-protein ligase RNF168 (chains A)
MGHHHHHHGSMALPKDAIPSLSECQCGICMEILVEPVTLPCNHTLCKPCFQSTVEKASLC
CPFCRRRVSSWTRYHTRRNSLVNVELWTIIQKHYPRECKLRASGQESEEVADDYQPVRLL
S

Ligands and cofactors

IDNameFormulaCopies
MLIMalonate ionC3 H2 O41
ZNZinc ionZn2

Primary citation

Structural basis for role of ring finger protein RNF168 RING domain. Zhang, X.Q., Chen, J., Wu, M. et al. Cell Cycle (2013) 12:312-321. DOI 10.4161/cc.23104 · PubMed

Other PDB entries of the same protein (UniProt Q8IYW5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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