5YUW: DNA polymerase IV - DNA ternary complex 6

DNA polymerase IV - DNA ternary complex 6. Determined by X-ray diffraction at 2.12 Å resolution. Released 7 Nov 2018.

Method
X-ray diffraction
Resolution
2.12 Å
Organisms
Escherichia coli K-12, Escherichia coli
Chains
6
Atoms
7,336
Mol. weight
103.3 kDa
Ligands
TTP, MG
Released
7 Nov 2018

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

Secondary structure: helices and β-sheets

5YUW contains 37 α-helices and 36 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: 18 helices, 18 β-strands

ElementResiduesLengthSheet
β-strand4-961
α-helix12-209
α-helix22-243
β-strand29-3242
β-strand4013
β-strand41-4442
α-helix46-494
β-strand5813
α-helix59-657
β-strand70-7232
α-helix76-9318
β-strand97-10151
β-strand104-10851
α-helix115-1173
α-helix119-13416
β-strand138-14361
α-helix146-1527
β-strand161-16331
α-helix166-1683
α-helix169-1746
β-strand17714
α-helix178-1803
α-helix186-1949
β-strand19914
α-helix200-2045
α-helix208-2158
α-helix217-2259
α-helix232-2343
β-strand242-253125
α-helix256-27722
β-strand28216
β-strand285-29285
β-strand297-30375
β-strand30616
α-helix309-32315
β-strand329-33795
Chain F: 19 helices, 18 β-strands
ElementResiduesLengthSheet
β-strand4-967
α-helix12-209
α-helix22-243
β-strand29-3248
β-strand4019
β-strand41-4448
α-helix46-494
β-strand5819
α-helix59-657
α-helix691
β-strand70-7238
α-helix76-9116
β-strand97-10157
β-strand104-10857
α-helix114-1174
α-helix119-13416
β-strand138-14367
α-helix146-1538
β-strand161-16337
α-helix169-1746
β-strand177110
α-helix178-1803
α-helix186-1949
β-strand199110
α-helix200-2045
α-helix208-2158
α-helix217-2259
α-helix232-2343
β-strand242-2531211
α-helix256-27722
β-strand282112
β-strand285-292811
β-strand297-303711
β-strand306112
α-helix309-32315
β-strand329-337911
α-helix338-3392

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA polymerase IVA, Fprotein352Escherichia coli K-12Q47155 (AlphaFold model)
DTN1B, GDNA18Escherichia coli
DTN2CC, HDNA19Escherichia coli
Sequence of entity 1 (A, F), FASTA
>5YUW_1 DNA polymerase IV (chains A, F)
GSRKIIHVDMDCFFAAVEMRDNPALRDIPIAIGGSRERRGVISTANYPARKFGVRSAMPT
GMALKLCPHLTLLPGRFDAYKEASNHIREIFSRYTSRIEPLSLDEAYLDVTDSVHCHGSA
TLIAQEIRQTIFNELQLTASAGVAPVKFLAKIASDMNKPNGQFVITPAEVPAFLQTLPLA
KIPGVGKVSAAKLEAMGLRTCGDVQKCDLVMLLKRFGKFGRILWERSQGIDERDVNSERL
RKSVGVERTMAEDIHHWSECEAIIERLYPELERRLAKVKPDLLIARQGVKLKFDDFQQTT
QEHVWPRLNKADLIATARKTWDERRGGRGVRLVGLHVTLLDPQMERQLVLGL
Sequence of entity 2 (B, G), FASTA
>5YUW_2 DTN1 (chains B, G)
TCTAGGGTCCTAGGACCC
Sequence of entity 3 (C, H), FASTA
>5YUW_3 DTN2C (chains C, H)
TCTAGGGTCCTAGGACCCT

Ligands and cofactors

IDNameFormulaCopies
TTPThymidine-5'-triphosphateC10 H17 N2 O14 P33
MGMagnesium ionMg4

Primary citation

Pyrophosphate hydrolysis is an intrinsic and critical step of the DNA synthesis reaction. Kottur, J., Nair, D.T. Nucleic Acids Res (2018) 46:5875-5885. DOI 10.1093/nar/gky402 · PubMed

Other PDB entries of the same protein (UniProt Q47155 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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