MolNFT v1 · #171996 · protein
The pointed end complex of dynactin with the P150 projection docked
6ZNO: “The pointed end complex of dynactin with the P150 projection docked”. Electron microscopy, 3 ligands (ADP, ATP, ZN). MolNFT v1 #171996 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6ZNO
- Type
- protein
- Length
- 2,697 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- F2Z5G5, Q6QAQ1, I3LHK5, A0A5G2QD80, D0G6S1, A0A286ZK88, A0A4X1TB62
- Ligands
- ADP, ATP, ZN
Structure
electron microscopy · 9 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| G, I | — | protein | 370 | — | F2Z5G5 |
| H | — | protein | 370 | — | Q6QAQ1 |
| J | — | protein | 379 | — | I3LHK5 |
| M | — | protein | 75 | — | A0A5G2QD80 |
| U | — | protein | 167 | — | D0G6S1 |
| V | — | protein | 179 | — | A0A286ZK88 |
| Y | — | protein | 410 | — | A0A4X1TB62 |
| Z | — | protein | 189 | — | — |
| z | — | protein | 188 | — | — |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 3 copies · chains G, I, J, Y
- ATP · Adenosine-5'-triphosphate · ligand · chains H
- ZN · Zinc ion · metal · 3 copies · chains Y
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 F2Z5G5
- Every structure of UniProt Q6QAQ1
- Every structure of UniProt I3LHK5
- Every structure of UniProt A0A5G2QD80
- Every structure of UniProt D0G6S1
- Every structure of UniProt A0A286ZK88
- Every structure of UniProt A0A4X1TB62
- Elsewhere: RCSB PDB 6ZNO · PDBe 6ZNO · UniProt F2Z5G5 · UniProt Q6QAQ1 · UniProt I3LHK5 · UniProt A0A5G2QD80 · UniProt D0G6S1 · UniProt A0A286ZK88 · UniProt A0A4X1TB62
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