5V86: DCN1

Structure of DCN1 bound to NAcM-OPT. Determined by X-ray diffraction at 1.37 Å resolution. Released 24 May 2017.

Method
X-ray diffraction
Resolution
1.37 Å
Organisms
Enterobacteria phage T4, Homo sapiens
Chains
1
Atoms
3,537
Mol. weight
44.61 kDa
Ligands
8ZA
Released
24 May 2017

Explore 5V86 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5V86 contains 20 α-helices and 12 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: 20 helices, 12 β-strands

ElementResiduesLengthSheet
α-helix-8--54
α-helix3-108
β-strand14-1521
β-strand1612
β-strand17-1931
β-strand25-2841
β-strand31-3441
α-helix39-5012
β-strand5712
α-helix60-7920
α-helix85-906
α-helix93-11220
α-helix115-1228
α-helix126-1338
α-helix137-1415
α-helix143-15513
α-helix159-107217
β-strand107413
β-strand107713
β-strand1080-108124
α-helix1083-109210
α-helix1100-11089
β-strand1117-111824
α-helix1119-112810
α-helix1134-114714
α-helix1153-116513
β-strand117315
α-helix1175-118612
α-helix1193-12019
β-strand120815
α-helix1210-122213
α-helix1238-124710

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Lysozyme,DCN1-like protein 1Aprotein384Enterobacteria phage T4, Homo sapiensP00720, Q96GG9 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5V86_1 Lysozyme,DCN1-like protein 1 (chains A)
MGSSHHHHHHSQDLENLYFQGSMNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPS
LNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAA
LINMVFQMGETGVAGFTNSLRMLQQKRWAEAAVNLAKSRWYNQTPNRTKRVITTFATGTW
DAYKNLRKKLEQLYNRYKDPQDENKIGIDGIQQFCDDLALDPASISVLIIAWKFRAATQC
EFSKQEFMDGMTELGCDSIEKLKAQIPKMEQELKEPGRFKDFYQFTFNFAKNPGQKGLDL
EMAIAYWNLVLNGRFKFLDLWNKFLLEHHKRSIPKDTWNLLLDFSTMIADDMSNYDEEGA
WPVLIDDFVEFARPQIAGTKSTTV

Ligands and cofactors

IDNameFormulaCopies
8ZAN-benzyl-N-(1-butylpiperidin-4-yl)-N'-(3,4-dichlorophenyl)ureaC23 H29 Cl2 N3 O1

Primary citation

Blocking an N-terminal acetylation-dependent protein interaction inhibits an E3 ligase. Scott, D.C., Hammill, J.T., Min, J. et al. Nat Chem Biol (2017) 13:850-857. DOI 10.1038/nchembio.2386 · PubMed

Other PDB entries of the same protein (UniProt P00720), best resolution first:

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