5YV3: DNA polymerase IV - DNA ternary complex 7

DNA polymerase IV - DNA ternary complex 7. Determined by X-ray diffraction at 2.03 Å resolution. Released 7 Nov 2018.

Method
X-ray diffraction
Resolution
2.03 Å
Organism
Escherichia coli K-12
Chains
6
Atoms
7,230
Mol. weight
102.99 kDa
Ligands
MG, TTP, DPO
Released
7 Nov 2018

Explore 5YV3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5YV3 contains 38 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: 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-helix76-9318
β-strand97-10157
β-strand104-10857
α-helix115-1173
α-helix119-13416
β-strand138-14367
α-helix146-15510
β-strand161-16337
α-helix166-1683
α-helix169-1746
β-strand177110
α-helix178-1803
α-helix186-1938
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
Chain F: 19 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-helix76-9116
β-strand97-10151
β-strand104-10851
α-helix114-1174
α-helix119-13416
β-strand138-14361
α-helix146-1538
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
α-helix338-3392

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA polymerase IVA, Fprotein352Escherichia coli K-12Q47155 (AlphaFold model)
DTN1B, GDNA18Escherichia coli K-12
DTN2C, HDNA19Escherichia coli K-12
Sequence of entity 1 (A, F), FASTA
>5YV3_1 DNA polymerase IV (chains A, F)
GSRKIIHVDMDCFFAAVEMRDNPALRDIPIAIGGSRERRGVISTANYPARKFGVRSAMPT
GMALKLCPHLTLLPGRFDAYKEASNHIREIFSRYTSRIEPLSLDEAYLDVTDSVHCHGSA
TLIAQEIRQTIFNELQLTASAGVAPVKFLAKIASDMNKPNGQFVITPAEVPAFLQTLPLA
KIPGVGKVSAAKLEAMGLRTCGDVQKCDLVMLLKRFGKFGRILWERSQGIDERDVNSERL
RKSVGVERTMAEDIHHWSECEAIIERLYPELERRLAKVKPDLLIARQGVKLKFDDFQQTT
QEHVWPRLNKADLIATARKTWDERRGGRGVRLVGLHVTLLDPQMERQLVLGL
Sequence of entity 2 (B, G), FASTA
>5YV3_2 DTN1 (chains B, G)
TCTAGGGTCCTAGGACCC
Sequence of entity 3 (C, H), FASTA
>5YV3_3 DTN2 (chains C, H)
TCTAGGGTCCTAGGACCCT

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg4
TTPThymidine-5'-triphosphateC10 H17 N2 O14 P32
DPODiphosphateO7 P21

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:

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