MolNFT v1 · #143531 · protein
Structure of full length human ampk (A2B2G1) in complex with a small molecule activator SC4.
6B2E: “Structure of full length human ampk (A2B2G1) in complex with a small molecule activator SC4.”. X-ray diffraction, 4 ligands (AMP, STU, CG7). MolNFT v1 #143531 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6B2E
- Type
- protein
- Length
- 931 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P54646, O43741, P54619
- Ligands
- AMP, STU, CG7, GLC
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 443 | — | P54646 |
| B | — | protein | 193 | — | O43741 |
| C | — | protein | 295 | — | P54619 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · 2 copies · chains A, C
- STU · Staurosporine · ligand · chains A
- CG7 · 5-{[6-chloro-5-(2'-hydroxy[1,1'-biphenyl]-4-yl)-1H-imidazo[4,5-b]pyridin-2-yl]oxy}-2-methylbenzoic acid · ligand · chains A, B
- GLC · alpha-D-glucopyranose · sugar · 7 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6B2E · Structure of full length human AMPK (a2b2g1) in complex with a small molecule activator… · the same entry in another collection · chain A against A, TM-score 1.00
- P54619 · AlphaFold monomer V2.0 prediction for 5'-AMP-activated protein kinase subunit gamma-1… · a predicted model of the same protein · chain C against A, TM-score 0.96
- P54646 · AlphaFold monomer V2.0 prediction for 5'-AMP-activated protein kinase catalytic subunit… · a predicted model of the same protein · chain A against A, TM-score 0.95
- O43741 · AlphaFold monomer V2.0 prediction for 5'-AMP-activated protein kinase subunit beta-2… · a predicted model of the same protein · chain B against A, TM-score 0.86
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 P54646
- Every structure of UniProt O43741
- Every structure of UniProt P54619
- Elsewhere: RCSB PDB 6B2E · PDBe 6B2E · UniProt P54646 · UniProt O43741 · UniProt P54619
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