MolNFT v1 · #172803 · protein + DNA + RNA
Cryo-EM structure of human RNA polymerase III elongation complex 1
7AE1: “Cryo-EM structure of human RNA polymerase III elongation complex 1”. Electron microscopy, 3 ligands (SF4, ZN, MG). MolNFT v1 #172803 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7AE1
- Type
- protein + DNA + RNA
- Length
- 5,287 residues
- Chains
- 20
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O14802, Q9NW08, O15160, O75575, P19388, P61218, Q9Y535, P52434, Q9Y2Y1, P62875, P0DPB6, P53803, Q9NVU0, P05423, Q9BUI4, Q9H1D9, O15318
- Ligands
- SF4, ZN, MG
Structure
electron microscopy · 20 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1381 | — | O14802 |
| B | — | protein | 1097 | — | Q9NW08 |
| C | — | protein | 343 | — | O15160 |
| D | — | protein | 124 | — | O75575 |
| E | — | protein | 209 | — | P19388 |
| F | — | protein | 78 | — | P61218 |
| G | — | protein | 189 | — | Q9Y535 |
| H | — | protein | 148 | — | P52434 |
| I | — | protein | 107 | — | Q9Y2Y1 |
| J | — | protein | 66 | — | P62875 |
| K | — | protein | 107 | — | P0DPB6 |
| L | — | protein | 46 | — | P53803 |
| M | — | protein | 400 | — | Q9NVU0 |
| N | — | protein | 186 | — | P05423 |
| O | — | protein | 512 | — | Q9BUI4 |
| P | — | protein | 146 | — | Q9H1D9 |
| Q | — | protein | 104 | — | O15318 |
| R | — | rna | 6 | — | — |
| S | — | dna | 15 | — | — |
| T | — | dna | 23 | — | — |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · chains O, P
- ZN · Zinc ion · metal · 7 copies · chains A, B, I, J, L
- MG · Magnesium ion · metal · chains A, R
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7AE1 · Cryo-EM structure of human RNA Polymerase III elongation complex 1 · the same entry in another collection · chain J against J, 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 O14802
- Every structure of UniProt Q9NW08
- Every structure of UniProt O15160
- Every structure of UniProt O75575
- Every structure of UniProt P19388
- Every structure of UniProt P61218
- Every structure of UniProt Q9Y535
- Every structure of UniProt P52434
- Every structure of UniProt Q9Y2Y1
- Every structure of UniProt P62875
- Every structure of UniProt P0DPB6
- Every structure of UniProt P53803
- Every structure of UniProt Q9NVU0
- Every structure of UniProt P05423
- Every structure of UniProt Q9BUI4
- Every structure of UniProt Q9H1D9
- Every structure of UniProt O15318
- Elsewhere: RCSB PDB 7AE1 · PDBe 7AE1 · UniProt O14802 · UniProt Q9NW08 · UniProt O15160 · UniProt O75575 · UniProt P19388 · UniProt P61218 · UniProt Q9Y535 · UniProt P52434 · UniProt Q9Y2Y1 · UniProt P62875 · UniProt P0DPB6 · UniProt P53803 · UniProt Q9NVU0 · UniProt P05423 · UniProt Q9BUI4 · UniProt Q9H1D9 · UniProt O15318
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