3HU3: P97 N-D1 R155H mutant

Structure of p97 N-D1 R155H mutant in complex with ATPgS. Determined by X-ray diffraction at 2.2 Å resolution. Released 16 Jun 2010.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Homo sapiens
Chains
2
Atoms
7,369
Mol. weight
110.22 kDa
Ligands
MG, AGS
Released
16 Jun 2010

Explore 3HU3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3HU3 contains 61 α-helices and 48 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: 31 helices, 24 β-strands

ElementResiduesLengthSheet
α-helix19-213
β-strand25-2951
β-strand38-4141
α-helix43-497
β-strand56-6051
β-strand66-7381
β-strand81-8331
α-helix86-916
β-strand99-10461
β-strand11012
β-strand113-11863
β-strand11914
α-helix120-1223
α-helix1301
α-helix131-1355
α-helix136-1394
β-strand144-14742
β-strand151-15663
β-strand159-169113
β-strand173-17642
β-strand181-18333
α-helix1881
β-strand18914
α-helix1901
α-helix191-1988
α-helix203-2053
α-helix210-2167
α-helix217-2215
α-helix222-2254
α-helix227-2337
α-helix236-2383
β-strand240-24455
α-helix251-26111
β-strand265-27065
α-helix271-2755
α-helix2781
α-helix281-29515
β-strand299-30465
α-helix306-3094
β-strand31116
α-helix319-33416
β-strand341-34775
α-helix350-3523
β-strand35316
α-helix355-3584
β-strand365-36845
α-helix374-38411
β-strand39017
α-helix396-4016
α-helix408-42417
α-helix439-4446
β-strand44717
α-helix449-4568
α-helix459-4657
α-helix466-4683
Chain B: 30 helices, 24 β-strands
ElementResiduesLengthSheet
α-helix19-213
β-strand25-2958
β-strand38-4148
α-helix43-497
β-strand56-6058
β-strand66-7388
β-strand81-8338
α-helix86-916
β-strand99-10468
α-helix1091
β-strand11019
α-helix1111
β-strand113-118610
β-strand119111
α-helix1301
α-helix131-1355
α-helix136-1394
β-strand144-14749
β-strand151-156610
β-strand159-1691110
β-strand173-17649
β-strand181-183310
α-helix187-1882
β-strand189111
α-helix1901
α-helix191-1988
α-helix203-2053
α-helix210-2167
α-helix217-2215
α-helix222-2254
α-helix227-2337
α-helix236-2383
β-strand240-244512
α-helix251-26111
β-strand265-270612
α-helix271-2755
α-helix2781
α-helix281-29515
β-strand299-304612
α-helix306-3094
β-strand311113
α-helix319-33416
β-strand341-347712
α-helix350-3523
β-strand353113
α-helix355-3584
β-strand365-368412
α-helix374-38411
β-strand390114
α-helix396-4016
α-helix408-42417
α-helix439-4446
β-strand447114
α-helix449-45810

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transitional endoplasmic reticulum ATPaseA, Bprotein489Homo sapiensP55072 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3HU3_1 Transitional endoplasmic reticulum ATPase (chains A, B)
MASGADSKGDDLSTAILKQKNRPNRLIVDEAINEDNSVVSLSQPKMDELQLFRGDTVLLK
GKKRREAVCIVLSDDTCSDEKIRMNRVVRNNLRVRLGDVISIQPCPDVKYGKRIHVLPID
DTVEGITGNLFEVYLKPYFLEAYRPIRKGDIFLVHGGMRAVEFKVVETDPSPYCIVAPDT
VIHCEGEPIKREDEEESLNEVGYDDIGGCRKQLAQIKEMVELPLRHPALFKAIGVKPPRG
ILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAI
IFIDELDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF
GRFDREVDIGIPDATGRLEILQIHTKNMKLADDVDLEQVANETHGHVGADLAALCSEAAL
QAIRKKMDLIDLEDETIDAEVMNSLAVTMDDFRWALSQSNPSALRETVVEVPQVTWEDIG
GRSHHHHHH

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg2
AGSPhosphothiophosphoric acid-adenylate esterC10 H16 N5 O12 P3 S2

Primary citation

A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants. Tang, W.K., Li, D., Li, C.C. et al. EMBO J (2010) 29:2217-2229. DOI 10.1038/emboj.2010.104 · PubMed

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

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