5YYD: DNA polymerase IV - ternary complex 15

DNA polymerase IV - ternary complex 15. Determined by X-ray diffraction at 2.05 Å resolution. Released 5 Sept 2018.

Method
X-ray diffraction
Resolution
2.05 Å
Organisms
Escherichia coli, Escherichia coli K-12
Chains
6
Atoms
7,116
Mol. weight
102.16 kDa
Ligands
TTW
Released
5 Sept 2018

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

Secondary structure: helices and β-sheets

5YYD contains 35 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-helix76-9015
β-strand97-10157
β-strand104-10857
α-helix115-1173
α-helix119-13416
β-strand138-14367
α-helix146-1538
β-strand161-16337
α-helix166-1683
α-helix169-1746
β-strand177110
α-helix178-1803
α-helix186-1938
β-strand199110
α-helix200-2045
α-helix209-2157
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: 16 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-helix169-1746
β-strand17714
α-helix178-1803
α-helix186-1949
β-strand19914
α-helix200-2045
α-helix208-2158
α-helix217-2259
β-strand242-253125
α-helix256-27722
β-strand28216
β-strand285-29285
β-strand297-30375
β-strand30616
α-helix309-32113
β-strand329-33795

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA polymerase IVA, Fprotein352Escherichia coliQ47155 (AlphaFold model)
DTN2B, C, G, HDNA18Escherichia coli K-12
Sequence of entity 1 (A, F), FASTA
>5YYD_1 DNA polymerase IV (chains A, F)
GSRKIIHVDMDCFFAAVEMRDNPALRDIPIAIGGSRERRGVISTANYPARKFGVRSAMPT
GMALKLCPHLTLLPGRFDAYKEASNHIREIFSRYTSRIEPLSLDEAYLDVTDSVHCHGSA
TLIAQEIRQTIFNELQLTASAGVAPVKFLAKIASDMNKPNGQFVITPAEVPAFLQTLPLA
KIPGVGKVSAAKLEAMGLRTCGDVQKCDLVMLLKRFGKFGRILWERSQGIDERDVNSERL
RKSVGVERTMAEDIHHWSECEAIIERLYPELERRLAKVKPDLLIARQGVKLKFDDFQQTT
QEHVWPRLNKADLIATARKTWDERRGGRGVRLVGLHVTLLDPQMERQLVLGL
Sequence of entity 2 (B, C, G, H), FASTA
>5YYD_2 DTN2 (chains B, C, G, H)
TCTAGGGTCCTAGGACCC

Ligands and cofactors

IDNameFormulaCopies
TTW5'-O-[hydroxy{[hydroxy(phosphonoamino)phosphoryl]oxy}phosphoryl]thymidineC10 H18 N3 O13 P32

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

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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