2NXP: NTD2 domain of the human TAF5 subunit of TFIID
Structure of NTD2 domain of the human TAF5 subunit of TFIID. Determined by X-ray diffraction at 2.17 Å resolution. Released 9 Jan 2007.
- Method
- X-ray diffraction
- Resolution
- 2.17 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 10,515
- Mol. weight
- 151.06 kDa
- Ligands
- CA
- Released
- 9 Jan 2007
Explore 2NXP in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2NXP contains 124 α-helices and 16 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: 15 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 198-202 | 5 | |
| α-helix | 203-205 | 3 | |
| α-helix | 214-226 | 13 | |
| α-helix | 230-236 | 7 | |
| α-helix | 237-239 | 3 | |
| α-helix | 240-253 | 14 | |
| α-helix | 257-267 | 11 | |
| α-helix | 268-270 | 3 | |
| α-helix | 273-275 | 3 | |
| α-helix | 276-283 | 8 | |
| α-helix | 288-291 | 4 | |
| α-helix | 295-300 | 6 | |
| α-helix | 302-304 | 3 | |
| β-strand | 306-310 | 5 | 1 |
| α-helix | 311-321 | 11 | |
| α-helix | 328-335 | 8 | |
| β-strand | 338-342 | 5 | 1 |
Chain B: 17 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 199-202 | 4 | |
| α-helix | 203-205 | 3 | |
| α-helix | 211-213 | 3 | |
| α-helix | 214-226 | 13 | |
| α-helix | 230-236 | 7 | |
| α-helix | 237-239 | 3 | |
| α-helix | 240-253 | 14 | |
| α-helix | 257-267 | 11 | |
| α-helix | 268-270 | 3 | |
| α-helix | 273-275 | 3 | |
| α-helix | 276-283 | 8 | |
| α-helix | 288-291 | 4 | |
| α-helix | 295-300 | 6 | |
| α-helix | 302-304 | 3 | |
| β-strand | 307-309 | 3 | 2 |
| α-helix | 311-322 | 12 | |
| α-helix | 328-331 | 4 | |
| α-helix | 332-336 | 5 | |
| β-strand | 339-341 | 3 | 2 |
Chain C: 16 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 198-202 | 5 | |
| α-helix | 203-205 | 3 | |
| α-helix | 211-213 | 3 | |
| α-helix | 214-226 | 13 | |
| α-helix | 230-236 | 7 | |
| α-helix | 237-239 | 3 | |
| α-helix | 240-253 | 14 | |
| α-helix | 257-267 | 11 | |
| α-helix | 268-270 | 3 | |
| α-helix | 273-275 | 3 | |
| α-helix | 276-283 | 8 | |
| α-helix | 288-291 | 4 | |
| α-helix | 295-300 | 6 | |
| α-helix | 302-304 | 3 | |
| β-strand | 306-310 | 5 | 3 |
| α-helix | 311-323 | 13 | |
| α-helix | 328-335 | 8 | |
| β-strand | 338-342 | 5 | 3 |
Chain D: 15 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 198-202 | 5 | |
| α-helix | 203-205 | 3 | |
| α-helix | 211-213 | 3 | |
| α-helix | 214-226 | 13 | |
| α-helix | 230-236 | 7 | |
| α-helix | 237-239 | 3 | |
| α-helix | 240-253 | 14 | |
| α-helix | 257-267 | 11 | |
| α-helix | 273-275 | 3 | |
| α-helix | 276-282 | 7 | |
| α-helix | 288-291 | 4 | |
| α-helix | 295-300 | 6 | |
| α-helix | 302-304 | 3 | |
| β-strand | 306-310 | 5 | 4 |
| α-helix | 311-323 | 13 | |
| α-helix | 328-335 | 8 | |
| β-strand | 338-342 | 5 | 4 |
Chain E: 16 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 198-202 | 5 | |
| α-helix | 203-205 | 3 | |
| α-helix | 211-213 | 3 | |
| α-helix | 214-226 | 13 | |
| α-helix | 230-236 | 7 | |
| α-helix | 237-239 | 3 | |
| α-helix | 240-253 | 14 | |
| α-helix | 257-267 | 11 | |
| α-helix | 268-270 | 3 | |
| α-helix | 273-275 | 3 | |
| α-helix | 276-282 | 7 | |
| α-helix | 288-291 | 4 | |
| α-helix | 295-299 | 5 | |
| α-helix | 302-304 | 3 | |
| β-strand | 306-310 | 5 | 5 |
| α-helix | 311-323 | 13 | |
| α-helix | 328-335 | 8 | |
| β-strand | 338-342 | 5 | 5 |
Chain F: 15 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 199-202 | 4 | |
| α-helix | 203-205 | 3 | |
| α-helix | 211-213 | 3 | |
| α-helix | 214-226 | 13 | |
| α-helix | 230-236 | 7 | |
| α-helix | 237-239 | 3 | |
| α-helix | 240-253 | 14 | |
| α-helix | 257-267 | 11 | |
| α-helix | 273-275 | 3 | |
| α-helix | 276-282 | 7 | |
| α-helix | 288-291 | 4 | |
| α-helix | 295-300 | 6 | |
| α-helix | 302-304 | 3 | |
| β-strand | 306-310 | 5 | 6 |
| α-helix | 311-321 | 11 | |
| α-helix | 328-335 | 8 | |
| β-strand | 338-342 | 5 | 6 |
Chain G: 16 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 199-202 | 4 | |
| α-helix | 203-205 | 3 | |
| α-helix | 211-213 | 3 | |
| α-helix | 214-226 | 13 | |
| α-helix | 230-236 | 7 | |
| α-helix | 237-239 | 3 | |
| α-helix | 240-253 | 14 | |
| α-helix | 257-267 | 11 | |
| α-helix | 268-270 | 3 | |
| α-helix | 273-275 | 3 | |
| α-helix | 276-283 | 8 | |
| α-helix | 288-291 | 4 | |
| α-helix | 295-299 | 5 | |
| α-helix | 302-304 | 3 | |
| β-strand | 306-310 | 5 | 7 |
| α-helix | 311-321 | 11 | |
| α-helix | 328-335 | 8 | |
| β-strand | 338-342 | 5 | 7 |
Chain H: 14 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 202-205 | 4 | |
| α-helix | 211-213 | 3 | |
| α-helix | 214-226 | 13 | |
| α-helix | 230-236 | 7 | |
| α-helix | 237-239 | 3 | |
| α-helix | 240-253 | 14 | |
| α-helix | 257-267 | 11 | |
| α-helix | 273-275 | 3 | |
| α-helix | 276-283 | 8 | |
| α-helix | 288-291 | 4 | |
| α-helix | 297-300 | 4 | |
| α-helix | 302-304 | 3 | |
| β-strand | 306-310 | 5 | 8 |
| α-helix | 311-321 | 11 | |
| α-helix | 328-335 | 8 | |
| β-strand | 338-342 | 5 | 8 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Transcription initiation factor TFIID subunit 5 | A, B, C, D, E, F, G, H | protein | 156 | Homo sapiens | Q15542 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA
>2NXP_1 Transcription initiation factor TFIID subunit 5 (chains A, B, C, D, E, F, G, H)
GSVAVEDQPDVSAVLSAYNQQGDPTMYEEYYSGLKHFIECSLDCHRAELSQLFYPLFVHM
YLELVYNQHENEAKSFFEKFHGDQECYYQDDLRVLSSLTKKEHMKGNETMLDFRTSKFVL
RISRDSYQLLKRHLQEKQNNQIWNIVQEHLYIDIFD
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| CA | Calcium ion | Ca | 8 |
Primary citation
Structural analysis and dimerization potential of the human TAF5 subunit of TFIID. Bhattacharya, S., Takada, S., Jacobson, R.H. Proc Natl Acad Sci U S A (2007) 104:1189-1194. DOI 10.1073/pnas.0610297104 · PubMed
Other PDB entries of the same protein (UniProt Q15542 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6F3T 2.5 Å, Crystal structure of the human TAF5-TAF6-TAF9 complex
- 7EGG 2.77 Å, TFIID lobe B subcomplex
- 7EGF 3.16 Å, TFIID lobe A subcomplex
- 7EGB 3.3 Å, TFIID-based holo PIC on SCP promoter
- 7EG9 3.7 Å, TFIID-based intermediate PIC on SCP promoter
- 7EGC 3.9 Å, p53-bound TFIID-based holo PIC on HDM2 promoter
- 7ENA 4.07 Å, TFIID-based PIC-Mediator holo-complex in pre-assembled state (pre-hPIC-MED)
- 7EGA 4.1 Å, TFIID-based intermediate PIC on PUMA promoter
- 7ENC 4.13 Å, TFIID-based PIC-Mediator holo-complex in fully-assembled state (hPIC-MED)
- 8GXS 4.16 Å, PIC-Mediator in complex with +1 nucleosome (T40N) in H-binding state
- 6MZC 4.5 Å, Human TFIID BC core
- 7EDX 4.5 Å, p53-bound TFIID-based core PIC on HDM2 promoter
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