MolNFT v2 · #151821 · protein + DNA + RNA
Yeast RNA polymerase I elongation complex stalled by cyclobutane pyrimidine dimer (CPD) with fully-ordered A49
6H68: “Yeast RNA polymerase I elongation complex stalled by cyclobutane pyrimidine dimer (CPD) with fully-ordered A49”. Electron microscopy at 4.6, 1 ligand (ZN). MolNFT v2 #151821 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6H68
- Type
- protein + DNA + RNA
- Length
- 4,564 residues
- Chains
- 17
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 4.6
- Source
- Saccharomyces cerevisiae (strain ATCC 204508 / S288c); SYNTHETIC CONSTRUCT
- UniProt
- P10964, P22138, P07703, P50106, P20434, P20435, P46669, P20436, P32529, P22139, P28000, P40422, Q01080, P47006
- Ligands
- ZN
Structure
electron microscopy · resolution 4.6 · 17 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1473 | — | P10964 |
| B | — | protein | 1175 | — | P22138 |
| C | — | protein | 306 | — | P07703 |
| D | — | protein | 59 | — | P50106 |
| E | — | protein | 215 | — | P20434 |
| F | — | protein | 100 | — | P20435 |
| G | — | protein | 201 | — | P46669 |
| H | — | protein | 132 | — | P20436 |
| I | — | protein | 65 | — | P32529 |
| J | — | protein | 69 | — | P22139 |
| K | — | protein | 103 | — | P28000 |
| L | — | protein | 45 | — | P40422 |
| M | — | protein | 396 | — | Q01080 |
| N | — | protein | 158 | — | P47006 |
| R | — | rna | 10 | — | — |
| T | — | dna | 33 | — | — |
| U | — | dna | 24 | — | — |
Ligands and binding sites
- ZN · Zinc ion · metal · 6 copies · chains A, B, I, J, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6H68 · Yeast RNA polymerase I elongation complex stalled by cyclobutane pyrimidine dimer (cpd)… · the same entry in another collection · chain U against U, 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 P10964
- Every structure of UniProt P22138
- Every structure of UniProt P07703
- Every structure of UniProt P50106
- Every structure of UniProt P20434
- Every structure of UniProt P20435
- Every structure of UniProt P46669
- Every structure of UniProt P20436
- Every structure of UniProt P32529
- Every structure of UniProt P22139
- Every structure of UniProt P28000
- Every structure of UniProt P40422
- Every structure of UniProt Q01080
- Every structure of UniProt P47006
- Elsewhere: RCSB PDB 6H68 · PDBe 6H68 · UniProt P10964 · UniProt P22138 · UniProt P07703 · UniProt P50106 · UniProt P20434 · UniProt P20435 · UniProt P46669 · UniProt P20436 · UniProt P32529 · UniProt P22139 · UniProt P28000 · UniProt P40422 · UniProt Q01080 · UniProt P47006
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