MolNFT v1 · #164836 · protein
Mouse RNF213 mutant R4753K modeling the moyamoya-disease-related human variant R4810K
6TAY: “Mouse RNF213 mutant R4753K modeling the moyamoya-disease-related human variant R4810K”. Electron microscopy, 3 ligands (ATP, ZN, MG). MolNFT v1 #164836 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6TAY
- Type
- protein
- Length
- 4,417 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- E9Q555
- Ligands
- ATP, ZN, MG
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 4417 | — | E9Q555 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- ZN · Zinc ion · metal · 2 copies · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 E9Q555
- Elsewhere: RCSB PDB 6TAY · PDBe 6TAY · UniProt E9Q555
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