1NGM: Yeast Brf1-TBP-DNA ternary complex

Crystal structure of a yeast Brf1-TBP-DNA ternary complex. Determined by X-ray diffraction at 2.95 Å resolution. Released 25 Mar 2003.

Method
X-ray diffraction
Resolution
2.95 Å
Organism
Saccharomyces cerevisiae
Chains
16
Atoms
10,800
Mol. weight
160.4 kDa
Released
25 Mar 2003

Explore 1NGM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1NGM contains 42 α-helices and 52 β-strands across 8 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: 5 helices, 12 β-strands

ElementResiduesLengthSheet
β-strand69-7571
α-helix82-865
β-strand93-9422
β-strand102-10322
β-strand11512
β-strand122-12651
α-helix130-1356
α-helix139-1468
β-strand153-15641
β-strand160-16121
β-strand163-16533
α-helix175-1784
β-strand183-18423
β-strand193-19643
β-strand203-20643
β-strand211-21333
α-helix220-23617
Chain B: 5 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix442-4443
α-helix448-4525
α-helix470-4723
α-helix477-49014
α-helix494-5007
Chain E: 5 helices, 11 β-strands
ElementResiduesLengthSheet
α-helix651
β-strand66-75104
α-helix82-865
β-strand8915
β-strand92-9434
β-strand101-10444
β-strand112-11654
β-strand120-12674
α-helix129-14618
β-strand153-165134
α-helix172-1776
β-strand183-18424
β-strand192-19654
β-strand203-20754
β-strand211-21774
α-helix220-23617
Chain F: 7 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix439-4402
α-helix442-4443
α-helix448-4525
α-helix463-4653
α-helix468-4714
β-strand47415
α-helix477-49014
α-helix492-50413
Chain I: 6 helices, 12 β-strands
ElementResiduesLengthSheet
α-helix651
β-strand66-75106
α-helix82-887
β-strand92-9546
β-strand99-10796
β-strand110-11676
β-strand120-12676
α-helix129-14618
β-strand153-165136
β-strand17017
α-helix172-1787
β-strand183-18426
β-strand193-19646
β-strand203-20646
β-strand211-21776
α-helix220-23011
α-helix232-2354
β-strand23817
Chain J: 4 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix462-4643
α-helix468-4714
α-helix477-49014
α-helix492-5009
Chain M: 5 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix651
β-strand66-75108
α-helix82-865
β-strand8919
β-strand9418
β-strand101-10448
β-strand107110
β-strand110110
β-strand112-11658
β-strand120-12678
α-helix129-14618
β-strand153-165138
β-strand170111
α-helix172-1787
β-strand184-186312
β-strand190-194512
β-strand20418
β-strand211-21448
α-helix222-23514
β-strand238111
Chain N: 5 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix463-4653
α-helix468-4703
β-strand47419
α-helix478-49013
α-helix492-4954
α-helix501-5044

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
5'-d(*cp*tp*ap*tp*ap*ap*ap*ap*ap*ap*ap*tp*gp*tp*tp*tp*tp*tp*t)-3'C, G, K, ODNA19
5'-d(*ap*ap*ap*ap*ap*ap*cp*ap*tp*tp*tp*tp*tp*tp*tp*ap*tp*ap*g)-3'D, H, L, PDNA19
Transcription initiation factor TFIIDA, E, I, Mprotein180Saccharomyces cerevisiaeP13393 (AlphaFold model)
Transcription factor IIIB BRF1 subunitB, F, J, Nprotein72Saccharomyces cerevisiaeP29056 (AlphaFold model)
Sequence of entity 1 (C, G, K, O), FASTA
>1NGM_1 5'-D(*CP*TP*AP*TP*AP*AP*AP*AP*AP*AP*AP*TP*GP*TP*TP*TP*TP*TP*T)-3' (chains C, G, K, O)
CTATAAAAAAATGTTTTTT
Sequence of entity 2 (D, H, L, P), FASTA
>1NGM_2 5'-D(*AP*AP*AP*AP*AP*AP*CP*AP*TP*TP*TP*TP*TP*TP*TP*AP*TP*AP*G)-3' (chains D, H, L, P)
AAAAAACATTTTTTTATAG
Sequence of entity 3 (A, E, I, M), FASTA
>1NGM_3 Transcription initiation factor TFIID (chains A, E, I, M)
SGIVPTLQNIVATVTLGCRLDLKTVALHARNAEYNPKRFAAVIMRIREPKTTALIFASGK
MVVTGAKSEDDSKLASRKYARIIQKIGFAAKFTDFKIQNIVGSCDVKFPIRLEGLAFSHG
TFSSYEPELFPGLIYRMVKPKIVLLIFVSGKIVLTGAKQREEIYQAFEAIYPVLSEFRKM
Sequence of entity 4 (B, F, J, N), FASTA
>1NGM_4 Transcription factor IIIB BRF1 subunit (chains B, F, J, N)
GSYCPRNLHLLPTTDTYLSKVSDDPDNLEDVDDEELNAHLLNEEASKLKERIWIGLNADF
LLEQESKRLKQE

Primary citation

Crystal structure of a transcription factor IIIB core interface ternary complex. Juo, Z.S., Kassavetis, G.A., Wang, J. et al. Nature (2003) 422:534-539. DOI 10.1038/nature01534 · PubMed

Other PDB entries of the same protein (UniProt P13393 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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