MolNFT v1 · #176156 · protein
Cryo-EM structure of the AMS1 and NBR1 complex
7DD9: “Cryo-EM structure of the AMS1 and NBR1 complex”. Electron microscopy, 1 ligand (ZN). MolNFT v1 #176156 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7DD9
- Type
- protein
- Length
- 4,516 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9UT61, Q9P792, P0AEX9
- Ligands
- ZN
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G | — | protein | 1129 | — | Q9UT61, Q9P792, P0AEX9 |
Ligands and binding sites
- ZN · Zinc ion · metal · 12 copies · chains A, C, E, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7DD9 · Cryo-EM structure of the Ams1 and Nbr1 complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UT61 · AlphaFold monomer V2.0 prediction for alpha-mannosidase (Q9UT61) · a predicted model of the same protein · chain A against A, TM-score 0.95
- Q9P792 · AlphaFold monomer V2.0 prediction for zz-type zinc finger-containing protein P35G2.11C… · a predicted model of the same protein · chain A against A, TM-score 0.15
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 Q9UT61
- Every structure of UniProt Q9P792
- Every structure of UniProt P0AEX9
- Elsewhere: RCSB PDB 7DD9 · PDBe 7DD9 · UniProt Q9UT61 · UniProt Q9P792 · UniProt P0AEX9
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