3EB5: CIAP2 RING domain

Structure of the cIAP2 RING domain. Determined by X-ray diffraction at 2.0 Å resolution. Released 9 Sept 2008.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
1
Atoms
551
Mol. weight
8.39 kDa
Ligands
ZN
Released
9 Sept 2008

Explore 3EB5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3EB5 contains 5 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: 5 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix544-55512
β-strand55611
β-strand56411
α-helix5651
β-strand567-57042
β-strand575-57732
α-helix582-5843
β-strand58713
α-helix5931
β-strand59413
α-helix5951
β-strand597-60042

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Baculoviral IAP repeat-containing protein 3Aprotein74Homo sapiensQ13489 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3EB5_1 Baculoviral IAP repeat-containing protein 3 (chains A)
LGSGTTEDVSDLPVEEQLRRLQEERTCKVCMDKEVSIVFIPCGHLVVCKDCAPSLRKCPI
CRSTIKGTVRTFLS

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2

Water and common crystallization additives (NA) are not listed.

Primary citation

Structures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitment. Mace, P.D., Linke, K., Feltham, R. et al. J Biol Chem (2008) 283:31633-31640. DOI 10.1074/jbc.M804753200 · PubMed

Other PDB entries of the same protein (UniProt Q13489 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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