Research workbench
Structure of ATATM3 in the outward-facing conformation
Analyse Structure of ATATM3 in the outward-facing conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N5B
- Type
- protein
- Length
- 1,160 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9LVM1
- Ligands
- ADP, MG, VO4
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 580 | — | Q9LVM1 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- VO4 · Vanadate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7N5B · Structure of AtAtm3 in the outward-facing conformation · the same entry in another collection · chain A against A, TM-score 1.00
- Q9LVM1 · AlphaFold monomer V2.0 prediction for ABC transporter B family member 25, mitochondrial… · a predicted model of the same protein · chain A against A, TM-score 0.82
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 Q9LVM1
- Elsewhere: RCSB PDB 7N5B · PDBe 7N5B · UniProt Q9LVM1
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