2XZP: Upf1 helicase

Upf1 helicase. Determined by X-ray diffraction at 2.72 Å resolution. Released 30 Mar 2011.

Method
X-ray diffraction
Resolution
2.72 Å
Organism
HOMO SAPIENS
Chains
1
Atoms
4,798
Mol. weight
70.51 kDa
Ligands
MLI
Released
30 Mar 2011

Explore 2XZP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2XZP contains 37 α-helices and 28 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: 37 helices, 28 β-strands

ElementResiduesLengthSheet
α-helix299-32224
β-strand326-32941
β-strand332-33541
β-strand341-34661
α-helix352-3554
α-helix356-3572
β-strand361-36661
β-strand374-38291
α-helix3891
β-strand390-39561
β-strand409-41351
α-helix414-4152
α-helix418-43215
β-strand43712
α-helix439-4457
α-helix4651
α-helix469-4713
α-helix473-48311
β-strand487-49153
α-helix498-51114
α-helix5161
β-strand517-52153
α-helix524-53613
β-strand541-54333
α-helix547-5493
α-helix557-5593
β-strand56013
α-helix561-5644
α-helix572-58312
α-helix589-60921
β-strand612-61653
α-helix618-6214
β-strand632-63543
α-helix638-6403
α-helix643-6508
β-strand65412
β-strand656-66163
α-helix673-6753
α-helix676-6805
α-helix684-6907
α-helix694-6952
β-strand696-69723
α-helix6981
β-strand700-70124
α-helix706-71611
β-strand722-72324
β-strand746-75055
β-strand756-75836
β-strand763-76536
α-helix767-78216
α-helix787-7893
β-strand790-79345
α-helix797-81014
α-helix815-8195
β-strand822-82435
α-helix826-8294
β-strand834-84075
α-helix851-8533
α-helix856-8638
β-strand866-87495
α-helix876-8794
α-helix883-89412
β-strand898-90035
α-helix903-9053
β-strand907-90825

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Regulator of nonsense transcripts 1Aprotein623HOMO SAPIENSQ92900 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2XZP_1 REGULATOR OF NONSENSE TRANSCRIPTS 1 (chains A)
GHMRYEDAYQYQNIFGPLVKLEADYDKKLKESQTQDNITVRWDLGLNKKRIAYFTLPKTD
SDMRLMQGDEICLRYKGDLAPLWKGIGHVIKVPDNYGDEIAIELRSSVGAPVEVTHNFQV
DFVWKSTSFDRMQSALKTFAVDETSVSGYIYHKLLGHEVEDVIIKCQLPKRFTAQGLPDL
NHSQVYAVKTVLQRPLSLIQGPPGTGKTVTSATIVYHLARQGNGPVLVCAPSNIAVDQLT
EKIHQTGLKVVRLCAKSREAIDSPVSFLALHNQIRNMDSMPELQKLQQLKDETGELSSAD
EKRYRALKRTAERELLMNADVICCTCVGAGDPRLAKMQFRSILIDESTQATEPECMVPVV
LGAKQLILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVVLGIRPIRLQVQYRMHPALSAF
PSNIFYEGSLQNGVTAADRVKKGFDFQWPQPDKPMFFYVTQGQEEIASSGTSYLNRTEAA
NVEKITTKLLKAGAKPDQIGIITPYEGQRSYLVQYMQFSGSLHTKLYQEVEIASVDAFQG
REKDFIILSCVRANEHQGIGFLNDPRRLNVALTRARYGVIIVGNPKALSKQPLWNHLLNY
YKEQKVLVEGPLNNLRESLMQFS

Ligands and cofactors

IDNameFormulaCopies
MLIMalonate ionC3 H2 O42

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

Primary citation

Molecular Mechanisms for the RNA-Dependent ATPase Activity of Upf1 and its Regulation by Upf2. Chakrabarti, S., Jayachandran, U., Bonneau, F. et al. Mol Cell (2011) 41:693. DOI 10.1016/J.MOLCEL.2011.02.010 · PubMed

Other PDB entries of the same protein (UniProt Q92900 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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