5DYG: P97 N-D1 L198W mutant

Structure of p97 N-D1 L198W mutant in complex with ADP. Determined by X-ray diffraction at 2.2 Å resolution. Released 10 Feb 2016.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Homo sapiens
Chains
1
Atoms
3,642
Mol. weight
52.82 kDa
Ligands
ADP
Released
10 Feb 2016

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

Secondary structure: helices and β-sheets

5DYG contains 27 α-helices and 24 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: 27 helices, 24 β-strands

ElementResiduesLengthSheet
β-strand25-3061
β-strand38-4141
α-helix43-497
β-strand56-6051
β-strand66-7381
β-strand81-8441
α-helix86-927
β-strand99-10461
β-strand11012
β-strand113-11863
β-strand11914
α-helix120-1234
α-helix1301
α-helix131-1355
α-helix136-1394
β-strand144-14742
β-strand151-15663
β-strand159-169113
β-strand173-17642
β-strand181-18333
α-helix187-1882
β-strand18914
α-helix1901
α-helix191-1933
α-helix203-2053
α-helix210-22516
α-helix229-2324
α-helix235-2384
β-strand240-24455
α-helix251-26212
β-strand265-27065
α-helix271-2755
α-helix2781
α-helix281-29515
β-strand299-30465
α-helix306-3083
β-strand31116
α-helix319-33315
α-helix335-3373
β-strand341-34775
β-strand35316
α-helix355-3584
β-strand365-36845
α-helix374-38512
β-strand389-39027
α-helix396-4027
α-helix408-43225
α-helix435-4373
α-helix439-4446
β-strand446-44727
α-helix449-4568

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transitional endoplasmic reticulum ATPaseAprotein468Homo sapiensP55072 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5DYG_1 Transitional endoplasmic reticulum ATPase (chains A)
MASGADSKGDDLSTAILKQKNRPNRLIVDEAINEDNSVVSLSQPKMDELQLFRGDTVLLK
GKKRREAVCIVLSDDTCSDEKIRMNRVVRNNLRVRLGDVISIQPCPDVKYGKRIHVLPID
DTVEGITGNLFEVYLKPYFLEAYRPIRKGDIFLVRGGMRAVEFKVVETDPSPYCIVAPDT
VIHCEGEPIKREDEEESWNEVGYDDIGGCRKQLAQIKEMVELPLRHPALFKAIGVKPPRG
ILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAI
IFIDELDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF
GRFDREVDIGIPDATGRLEILQIHTKNMKLADDVDLEQVANETHGHVGADLAALCSEAAL
QAIRKKMDLIDLEDETIDAEVMNSLAVTMDDFRWALSQSNRSHHHHHH

Ligands and cofactors

IDNameFormulaCopies
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P21

Primary citation

Role of the D1-D2 Linker of Human VCP/p97 in the Asymmetry and ATPase Activity of the D1-domain. Tang, W.K., Xia, D. Sci Rep (2016) 6:20037-20037. DOI 10.1038/srep20037 · PubMed

Other PDB entries of the same protein (UniProt P55072 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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