Research workbench
P53-bound tfiid-based core pic on HDM2 promoter
Analyse P53-bound tfiid-based core pic on HDM2 promoter in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EDX
- Type
- protein + DNA
- Length
- 9,991 residues
- Chains
- 39
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription initiation factor tfiid subunit 1; Transcription initiation factor tfiid…
- EC
- 2.3.1.48, 2.7.11.1, 3.6.4.12, 2.7.7.6
- UniProt
- P21675, Q6P1X5, O00268, Q15542, P49848, Q15545, Q7Z7C8, Q16594, Q12962, Q16514, P52657, P20226, P52655, Q00403, P35269, P13984, Q5VWG9, Q15544, Q15543, A0A4X1TVZ5, I3LCH3, A0A481BYI6, A0A4X1VTX4, A0A4X1VEK9, A0A4X1ULF2, P60899, A0A4X1UK25, A0A4X1TRS6, A0A4X1VKG7
- Ligands
- ZN, MG
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 39 distinct chains · 35% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcription initiation factor tfiid subunit 1 (EC 2.3.1.48, 2.7.11.1) | protein | 602 | 33% helix, 13% strand | P21675 |
| B | Transcription initiation factor tfiid subunit 2 | protein | 963 | 40% helix, 20% strand | Q6P1X5 |
| D | Transcription initiation factor tfiid subunit 4 | protein | 165 | 65% helix, 2% strand | O00268 |
| E | Transcription initiation factor tfiid subunit 5 | protein | 546 | 22% helix, 29% strand | Q15542 |
| F | Transcription initiation factor tfiid subunit 6 | protein | 404 | 57% helix, 2% strand | P49848 |
| G | Transcription initiation factor tfiid subunit 7 | protein | 145 | 21% helix, 34% strand | Q15545 |
| H | Transcription initiation factor tfiid subunit 8 | protein | 209 | 44% helix, 2% strand | Q7Z7C8 |
| I | Transcription initiation factor tfiid subunit 9 | protein | 120 | 51% helix, 2% strand | Q16594 |
| J | Transcription initiation factor tfiid subunit 10 | protein | 89 | 53% helix, 3% strand | Q12962 |
| L | Transcription initiation factor tfiid subunit 12 | protein | 76 | 64% helix, 1% strand | Q16514 |
| O | Transcription initiation factor iia subunit 2 | protein | 97 | 38% helix, 29% strand | P52657 |
| P | Tata-box-binding protein | protein | 177 | 28% helix, 34% strand | P20226 |
| Q | Transcription initiation factor iia subunit 1 | protein | 122 | 40% helix, 32% strand | P52655 |
| R | Transcription initiation factor iib (EC 2.3.1.48) | protein | 248 | 55% helix, 4% strand | Q00403 |
| S | General transcription factor iif subunit 1 | protein | 134 | 19% helix, 39% strand | P35269 |
| T | General transcription factor iif subunit 2 (EC 3.6.4.12) | protein | 113 | 16% helix, 49% strand | P13984 |
| X | DNA (84-mer) | dna | 77 | — | — |
| Y | DNA (84-mer) | dna | 77 | — | — |
| c | Transcription initiation factor tfiid subunit 3 | protein | 127 | 53% helix, 3% strand | Q5VWG9 |
| d | Transcription initiation factor tfiid subunit 4 | protein | 158 | 53% helix, 4% strand | O00268 |
| e | Transcription initiation factor tfiid subunit 5 | protein | 539 | 13% helix, 26% strand | Q15542 |
| f | Transcription initiation factor tfiid subunit 6 | protein | 403 | 54% helix, 4% strand | P49848 |
| i | Transcription initiation factor tfiid subunit 9 | protein | 121 | 45% helix, 3% strand | Q16594 |
| j | Transcription initiation factor tfiid subunit 10 | protein | 95 | 46% helix, 3% strand | Q12962 |
| k | Transcription initiation factor tfiid subunit 11 | protein | 98 | 63% helix, 0% strand | Q15544 |
| l | Transcription initiation factor tfiid subunit 12 | protein | 107 | 57% helix, 3% strand | Q16514 |
| m | Transcription initiation factor tfiid subunit 13 | protein | 87 | 39% helix, 1% strand | Q15543 |
| o | RPB1 | protein | 1427 | 36% helix, 14% strand | — |
| p | DNA-directed RNA polymerase subunit beta (EC 2.7.7.6) | protein | 1134 | 25% helix, 23% strand | A0A4X1TVZ5 |
| q | DNA-directed RNA polymerase II subunit RPB3 | protein | 257 | 16% helix, 26% strand | I3LCH3 |
| r | DNA-directed RNA polymerase II subunit RPB4 | protein | 128 | 52% helix, 1% strand | A0A481BYI6 |
| s | DNA-directed RNA polymerase II subunit E | protein | 209 | 33% helix, 20% strand | A0A4X1VTX4 |
| t | DNA-directed RNA polymerase II subunit F | protein | 79 | 35% helix, 18% strand | A0A4X1VEK9 |
| v | DNA-directed RNA polymerases I, II, and III subunit RPABC3 | protein | 148 | 0% helix, 47% strand | A0A4X1ULF2 |
| w | DNA-directed RNA polymerase II subunit RPB9 | protein | 114 | 7% helix, 27% strand | P60899 |
| x | RPB10 | protein | 64 | 39% helix, 3% strand | — |
| y | RNA_POL_L_2 domain-containing protein | protein | 117 | 38% helix, 19% strand | A0A4X1UK25 |
| z | RPB12 | protein | 44 | 0% helix, 30% strand | A0A4X1TRS6 |
| u | DNA-directed RNA polymerase II subunit RPB7 | protein | 171 | 10% helix, 52% strand | A0A4X1VKG7 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1180 | 0.86 | 0.87 | 116 | empty |
| 2 | 1030 | 0.86 | 0.87 | 96 | empty |
| 3 | 1193 | 0.86 | 0.87 | 118 | empty |
| 4 | 832 | 0.86 | 0.88 | 96 | empty |
| 5 | 1071 | 0.85 | 0.86 | 129 | empty |
Interfaces
109 interfaces between chains.
- o–p · 8108 Ų buried · 82 hydrogen bonds · protein-protein
- A–G · 4954 Ų buried · 78 hydrogen bonds · protein-protein
- X–Y · 3536 Ų buried · 354 hydrogen bonds · nucleic-nucleic
- O–Q · 2646 Ų buried · 38 hydrogen bonds · protein-protein
- c–j · 2643 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 7EDX · p53-bound TFIID-based core PIC on HDM2 promoter · the same entry in another collection · chain O against O, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P21675
- Every structure of UniProt Q6P1X5
- Every structure of UniProt O00268
- Every structure of UniProt Q15542
- Every structure of UniProt P49848
- Every structure of UniProt Q15545
- Every structure of UniProt Q7Z7C8
- Every structure of UniProt Q16594
- Every structure of UniProt Q12962
- Every structure of UniProt Q16514
- Every structure of UniProt P52657
- Every structure of UniProt P20226
- Every structure of UniProt P52655
- Every structure of UniProt Q00403
- Every structure of UniProt P35269
- Every structure of UniProt P13984
- Every structure of UniProt Q5VWG9
- Every structure of UniProt Q15544
- Every structure of UniProt Q15543
- Every structure of UniProt A0A4X1TVZ5
- Every structure of UniProt I3LCH3
- Every structure of UniProt A0A481BYI6
- Every structure of UniProt A0A4X1VTX4
- Every structure of UniProt A0A4X1VEK9
- Every structure of UniProt A0A4X1ULF2
- Every structure of UniProt P60899
- Every structure of UniProt A0A4X1UK25
- Every structure of UniProt A0A4X1TRS6
- Every structure of UniProt A0A4X1VKG7
- Elsewhere: RCSB PDB 7EDX · PDBe 7EDX · UniProt P21675 · UniProt Q6P1X5 · UniProt O00268 · UniProt Q15542 · UniProt P49848 · UniProt Q15545 · UniProt Q7Z7C8 · UniProt Q16594 · UniProt Q12962 · UniProt Q16514 · UniProt P52657 · UniProt P20226 · UniProt P52655 · UniProt Q00403 · UniProt P35269 · UniProt P13984 · UniProt Q5VWG9 · UniProt Q15544 · UniProt Q15543 · UniProt A0A4X1TVZ5 · UniProt I3LCH3 · UniProt A0A481BYI6 · UniProt A0A4X1VTX4 · UniProt A0A4X1VEK9 · UniProt A0A4X1ULF2 · UniProt P60899 · UniProt A0A4X1UK25 · UniProt A0A4X1TRS6 · UniProt A0A4X1VKG7
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