Research workbench
Crystal structure of the human tfiie complex
Analyse Crystal structure of the human tfiie complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5GPY
- Type
- protein
- Length
- 278 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- General transcription factor iie subunit 1; Transcription initiation factor iie subunit…
- UniProt
- P29083, P29084
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | General transcription factor iie subunit 1 | protein | 177 | 55% helix, 18% strand | P29083 |
| B | Transcription initiation factor iie subunit beta | protein | 101 | 50% helix, 12% strand | P29084 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 203 | 0.64 | 0.84 | 32 | empty |
Interfaces
1 interface between chains.
- A–B · 2002 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 5GPY · Crystal structure of the human TFIIE complex · the same entry in another collection · chain A against A, TM-score 1.00
- P29084 · AlphaFold monomer V2.0 prediction for transcription initiation factor iie subunit beta… · a predicted model of the same protein · chain B against A, TM-score 0.97
- P29083 · AlphaFold monomer V2.0 prediction for general transcription factor iie subunit 1 (P29083) · a predicted model of the same protein · chain A against A, TM-score 0.82
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 P29083
- Every structure of UniProt P29084
- Elsewhere: RCSB PDB 5GPY · PDBe 5GPY · UniProt P29083 · UniProt P29084
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