MolNFT v1 · #152736 · protein + DNA
The crosslinked complex of iswi-nucleosome in the ADP-bound state
6IRO: “The crosslinked complex of iswi-nucleosome in the ADP-bound state”. Electron microscopy, 1 ligand (ADP). MolNFT v1 #152736 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6IRO
- Type
- protein + DNA
- Length
- 1,554 residues
- Chains
- 11
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P38144, A0A310TTQ1, P62799, Q6AZJ8, P02281
- Ligands
- ADP
Structure
electron microscopy · 9 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | — | protein | 496 | — | P38144 |
| A | — | protein | 98 | — | A0A310TTQ1 |
| B | — | protein | 87 | — | P62799 |
| C, G | — | protein | 107 | — | Q6AZJ8 |
| D, H | — | protein | 93 | — | P02281 |
| E | — | protein | 95 | — | A0A310TTQ1 |
| F | — | protein | 86 | — | P62799 |
| I | — | dna | 146 | — | — |
| J | — | dna | 146 | — | — |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6IRO · the crosslinked complex of ISWI-nucleosome in the ADP-bound state · the same entry in another collection · chain J against J, TM-score 1.00
- P38144 · AlphaFold monomer V2.0 prediction for iswi chromatin-remodeling complex ATPase ISW1… · a predicted model of the same protein · chain L against A, TM-score 0.81
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 P38144
- Every structure of UniProt A0A310TTQ1
- Every structure of UniProt P62799
- Every structure of UniProt Q6AZJ8
- Every structure of UniProt P02281
- Elsewhere: RCSB PDB 6IRO · PDBe 6IRO · UniProt P38144 · UniProt A0A310TTQ1 · UniProt P62799 · UniProt Q6AZJ8 · UniProt P02281
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