6IG1: DNA polymerase IV - DNA ternary complex 10

DNA polymerase IV - DNA ternary complex 10. Determined by X-ray diffraction at 1.97 Å resolution. Released 28 Nov 2018.

Method
X-ray diffraction
Resolution
1.97 Å
Organism
Escherichia coli K-12
Chains
6
Atoms
7,308
Mol. weight
103.78 kDa
Ligands
TTP, DPO, MG
Released
28 Nov 2018

Explore 6IG1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6IG1 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: 18 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
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-helix186-1949
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
Chain F: 20 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
α-helix691
β-strand70-7232
α-helix76-9116
β-strand97-10151
β-strand104-10851
α-helix114-1174
α-helix119-13416
β-strand138-14361
α-helix146-15510
β-strand161-16331
α-helix166-1683
α-helix169-1746
β-strand17714
α-helix178-1803
α-helix186-1938
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-helix309-32113
β-strand329-33795
α-helix338-3392

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA polymerase IVA, Fprotein352Escherichia coli K-12Q47155 (AlphaFold model)
DTN3B, C, G, HDNA19Escherichia coli K-12
Sequence of entity 1 (A, F), FASTA
>6IG1_1 DNA polymerase IV (chains A, F)
GSRKIIHVDMDCFFAAVEMRDNPALRDIPIAIGGSRERRGVISTANYPARKFGVRSAMPT
GMALKLCPHLTLLPGRFDAYKEASNHIREIFSRYTSRIEPLSLDEAYLDVTDSVHCHGSA
TLIAQEIRQTIFNELQLTASAGVAPVKFLAKIASDMNKPNGQFVITPAEVPAFLQTLPLA
KIPGVGKVSAAKLEAMGLRTCGDVQKCDLVMLLKRFGKFGRILWERSQGIDERDVNSERL
RKSVGVERTMAEDIHHWSECEAIIERLYPELERRLAKVKPDLLIARQGVKLKFDDFQQTT
QEHVWPRLNKADLIATARKTWDERRGGRGVRLVGLHVTLLDPQMERQLVLGL
Sequence of entity 2 (B, C, G, H), FASTA
>6IG1_2 DTN3 (chains B, C, G, H)
TCTAGGGTCCTAGGACCCT

Ligands and cofactors

IDNameFormulaCopies
TTPThymidine-5'-triphosphateC10 H17 N2 O14 P32
DPODiphosphateO7 P22
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:

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