MolNFT v1 · #187230 · protein
Human katp channel in open conformation, focused on kir and one sur, position 5
7S61: “Human katp channel in open conformation, focused on kir and one sur, position 5”. Electron microscopy, 3 ligands (ADP, ATP, MG). MolNFT v1 #187230 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7S61
- Type
- protein
- Length
- 2,676 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- B2RC52, Q09428
- Ligands
- ADP, ATP, MG
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 321 | — | B2RC52 |
| E | — | protein | 1392 | — | Q09428 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains E
- ATP · Adenosine-5'-triphosphate · ligand · chains E
- MG · Magnesium ion · metal · 2 copies · chains E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7S61 · Human KATP channel in open conformation, focused on Kir and one SUR, position 5 · the same entry in another collection · chain A against A, TM-score 1.00
- Q09428 · AlphaFold monomer V2.0 prediction for ATP-binding cassette sub-family C member 8 (Q09428) · a predicted model of the same protein · chain E against A, TM-score 0.87
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 B2RC52
- Every structure of UniProt Q09428
- Elsewhere: RCSB PDB 7S61 · PDBe 7S61 · UniProt B2RC52 · UniProt Q09428
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