6R5E: Pri1 subunit of human primase

Crystal structure of the Pri1 subunit of human primase bound to 2F-ATP. Determined by X-ray diffraction at 1.85 Å resolution. Released 11 Sept 2019.

Method
X-ray diffraction
Resolution
1.85 Å
Organism
Homo sapiens
Chains
2
Atoms
7,007
Mol. weight
99.46 kDa
Ligands
ZN, MN, JSQ
Released
11 Sept 2019

Explore 6R5E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6R5E contains 58 α-helices and 27 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: 29 helices, 14 β-strands

ElementResiduesLengthSheet
α-helix9-157
α-helix16-205
α-helix23-308
α-helix32-343
β-strand43-4861
α-helix50-523
β-strand54-5851
α-helix63-7311
β-strand77-8481
α-helix88-936
α-helix951
β-strand101-10331
β-strand106-11162
α-helix112-1187
α-helix133-14412
α-helix145-1495
β-strand155-15952
β-strand164-16962
α-helix172-1754
α-helix179-18911
α-helix208-2092
α-helix210-22314
α-helix224-2307
α-helix237-2448
α-helix249-2513
α-helix252-26110
α-helix265-27612
α-helix291-30111
β-strand30512
α-helix307-3115
β-strand317-31821
α-helix3191
β-strand32313
β-strand32914
β-strand33013
β-strand33312
α-helix336-3416
α-helix344-3463
α-helix3481
β-strand34914
α-helix350-3578
α-helix383-3853
α-helix389-40618
Chain E: 29 helices, 13 β-strands
ElementResiduesLengthSheet
α-helix6-83
α-helix9-1911
α-helix23-319
α-helix32-343
β-strand43-4865
α-helix50-523
β-strand54-5855
α-helix63-7311
β-strand77-8485
α-helix88-936
β-strand101-10335
β-strand106-11166
α-helix112-1187
α-helix133-14412
α-helix145-1495
β-strand155-15956
β-strand164-16966
α-helix172-1754
α-helix179-18911
α-helix208-2092
α-helix210-22314
α-helix224-2307
α-helix237-2448
α-helix249-2513
α-helix252-26110
α-helix265-27713
α-helix291-30111
α-helix307-3115
β-strand317-31825
α-helix3191
β-strand32317
β-strand32918
β-strand33017
β-strand33316
α-helix336-3416
α-helix344-3463
α-helix3481
β-strand34918
α-helix350-3567
α-helix357-3593
α-helix383-3853
α-helix389-40517

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA primase small subunitA, Eprotein410Homo sapiensP49642 (AlphaFold model)
Sequence of entity 1 (A, E), FASTA
>6R5E_1 DNA primase small subunit (chains A, E)
GTSMETFDPTELPELLKLYYRRLFPYSQYYRWLNYGGVIKNYFQHREFSFTLKDDIYIRY
QSFNNQSDLEKEMQKMNPYKIDIGAVYSHRPNQHNTVKLGAFQAQEKELVFDIDMTDYDD
VRRCCSSADICPKCWTLMTMAIRIIDRALKEDFGFKHRLWVYSGRRGVHCWVCDESVRKL
SSAVRSGIVEYLSLVKGGQDVKKKVHLSEKIHPFIRKSINIIKKYFEEYALVNQDILENK
ESWDKILALVPETIHDELQQSFQKSHNSLQRWEHLKKVASRYQNNIKNDKYGPWLEWEIM
LQYCFPRLDINVSKGINHLLKSPFSVHPKTGRISVPIDLQKVDQFDPFTVPTISFICREL
DAISTNEEEKEENEAESDVKHRTRDYKKTSLAPYVKVFEHFLENLDKSRK

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2
MNManganese (II) ionMn4
JSQ2-fluoro-ATPC10 H15 F N5 O13 P32

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

Primary citation

Structural Basis for Inhibition of Human Primase by Arabinofuranosyl Nucleoside Analogues Fludarabine and Vidarabine. Holzer, S., Rzechorzek, N.J., Short, I.R. et al. ACS Chem Biol (2019) 14:1904-1912. DOI 10.1021/acschembio.9b00367 · PubMed

Other PDB entries of the same protein (UniProt P49642 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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