MolNFT v1 · #169232 · protein + DNA + RNA
Mfd-bound E.COLI RNA polymerase elongation complex - V state
6X50: “Mfd-bound E.COLI RNA polymerase elongation complex - V state”. Electron microscopy, 3 ligands (ATP, MG, ZN). MolNFT v1 #169232 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6X50
- Type
- protein + DNA + RNA
- Length
- 4,428 residues
- Chains
- 9
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A024L3Y3, A0A073G207, P0A8V4, A0A4S1NBU2, P0A802
- Ligands
- ATP, MG, ZN
Structure
electron microscopy · 9 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1143 | — | A0A024L3Y3 |
| G | — | protein | 224 | — | A0A073G207 |
| H | — | protein | 217 | — | A0A073G207 |
| I | — | protein | 1316 | — | P0A8V4 |
| J | — | protein | 1336 | — | A0A4S1NBU2 |
| K | — | protein | 79 | — | P0A802 |
| R | — | rna | 9 | — | — |
| P | — | dna | 55 | — | — |
| Q | — | dna | 49 | — | — |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A, J, R
- ZN · Zinc ion · metal · 2 copies · chains J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- P0A802 · AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit omega (P0A802) · a predicted model of the same protein · chain K against A, TM-score 0.94
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 A0A024L3Y3
- Every structure of UniProt A0A073G207
- Every structure of UniProt P0A8V4
- Every structure of UniProt A0A4S1NBU2
- Every structure of UniProt P0A802
- Elsewhere: RCSB PDB 6X50 · PDBe 6X50 · UniProt A0A024L3Y3 · UniProt A0A073G207 · UniProt P0A8V4 · UniProt A0A4S1NBU2 · UniProt P0A802
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