MolNFT v1 · #178182 · protein + DNA
Cryo-EM structure of spx-dependent transcription activation complex
7F75: “Cryo-EM structure of spx-dependent transcription activation complex”. Electron microscopy, 2 ligands (ZN, MG). MolNFT v1 #178182 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7F75
- Type
- protein + DNA
- Length
- 3,532 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P20429, P37870, P37871, O35011, P06224, O31718, P12464
- Ligands
- ZN, MG
Structure
electron microscopy · 12 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 224 | — | P20429 |
| B | — | protein | 220 | — | P20429 |
| C | — | protein | 1133 | — | P37870 |
| D | — | protein | 1142 | — | P37871 |
| E | — | protein | 62 | — | O35011 |
| F | — | protein | 272 | — | P06224 |
| H | — | protein | 69 | — | O31718 |
| G | — | protein | 129 | — | — |
| I | — | protein | 67 | — | P20429 |
| J | — | dna | 59 | — | — |
| K | — | dna | 63 | — | — |
| L | — | protein | 92 | — | P12464 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7F75 · Cryo-EM structure of Spx-dependent transcription activation complex · the same entry in another collection · chain L against L, 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 P20429
- Every structure of UniProt P37870
- Every structure of UniProt P37871
- Every structure of UniProt O35011
- Every structure of UniProt P06224
- Every structure of UniProt O31718
- Every structure of UniProt P12464
- Elsewhere: RCSB PDB 7F75 · PDBe 7F75 · UniProt P20429 · UniProt P37870 · UniProt P37871 · UniProt O35011 · UniProt P06224 · UniProt O31718 · UniProt P12464
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