3EG6: WDR5

Structure of WDR5 bound to MLL1 peptide. Determined by X-ray diffraction at 1.72 Å resolution. Released 30 Sept 2008.

Method
X-ray diffraction
Resolution
1.72 Å
Organism
Homo sapiens
Chains
2
Atoms
2,727
Mol. weight
35.93 kDa
Released
30 Sept 2008

Explore 3EG6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3EG6 contains 2 α-helices and 28 β-strands across 2 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: 1 helix, 28 β-strands

ElementResiduesLengthSheet
β-strand36-4161
β-strand48-5362
β-strand59-6462
β-strand69-7352
β-strand79-8352
β-strand90-9563
β-strand101-10663
β-strand110-11563
β-strand121-12663
β-strand132-13764
β-strand143-14864
β-strand153-15754
β-strand162-16764
β-strand174-17965
β-strand185-19065
β-strand195-19955
β-strand205-20955
α-helix215-2162
β-strand217-22266
β-strand228-23366
β-strand237-24266
β-strand247-25266
β-strand264-26747
β-strand273-27757
β-strand283-28757
β-strand293-29757
β-strand304-30961
β-strand315-32061
β-strand327-33151
Chain C: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix3764-37663

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
WD repeat-containing protein 5Aprotein312Homo sapiensP61964 (AlphaFold model)
MLL-1 peptideCprotein13Q03164
Sequence of entity 1 (A), FASTA
>3EG6_1 WD repeat-containing protein 5 (chains A)
ATQSKPTPVKPNYALKFTLAGHTKAVSSVKFSPNGEWLASSSADKLIKIWGAYDGKFEKT
ISGHKLGISDVAWSSDSNLLVSASDDKTLKIWDVSSGKCLKTLKGHSNYVFCCNFNPQSN
LIVSGSFDESVRIWDVKTGKCLKTLPAHSDPVSAVHFNRDGSLIVSSSYDGLCRIWDTAS
GQCLKTLIDDDNPPVSFVKFSPNGKYILAATLDNTLKLWDYSKGKCLKTYTGHKNEKYCI
FANFSVTGGKWIVSGSEDNLVYIWNLQTKEIVQKLQGHTDVVISTACHPTENIIASAALE
NDKTIKLWKSDC
Sequence of entity 2 (C), FASTA
>3EG6_2 MLL-1 peptide (chains C)
XGSARAEVHLRKS

Primary citation

Structure of WDR5 bound to mixed lineage leukemia protein-1 peptide. Patel, A., Dharmarajan, V., Cosgrove, M.S. J Biol Chem (2008) 283:32158-32161. DOI 10.1074/jbc.C800164200 · PubMed

Other PDB entries of the same protein (UniProt P61964 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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