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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：Q13131 New Search
11PDB entries
14Biological assembly
23chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
4RED Crystal structure of human AMPK alpha1 KD-AID with K43A mutation Deposited 2014-09-22 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 22–362（341 aa） Fragment：human AMPK KD-AID, UNP residues 22-362
Chain B 22–362（341 aa） Fragment：human AMPK KD-AID, UNP residues 22-362
Mutation：K43A Mutation：K43A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；0.5 M HNa2PO4/0.5 M HK2PO4, 0.1 M Tris hydrochloride, pH 8.5, 0.1 M H(NH4)2PO4, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.95 Å R-free 0.277
4RED Crystal structure of human AMPK alpha1 KD-AID with K43A mutation Deposited 2014-09-22 Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 22–362（341 aa） Fragment：human AMPK KD-AID, UNP residues 22-362
Chain B 22–362（341 aa） Fragment：human AMPK KD-AID, UNP residues 22-362
Mutation：K43A Mutation：K43A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；0.5 M HNa2PO4/0.5 M HK2PO4, 0.1 M Tris hydrochloride, pH 8.5, 0.1 M H(NH4)2PO4, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.95 Å R-free 0.277
4RED Crystal structure of human AMPK alpha1 KD-AID with K43A mutation Deposited 2014-09-22 Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 22–362（341 aa） Fragment：human AMPK KD-AID, UNP residues 22-362
Chain B 22–362（341 aa） Fragment：human AMPK KD-AID, UNP residues 22-362
Mutation：K43A Mutation：K43A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；0.5 M HNa2PO4/0.5 M HK2PO4, 0.1 M Tris hydrochloride, pH 8.5, 0.1 M H(NH4)2PO4, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.95 Å R-free 0.277
4RER Crystal structure of the phosphorylated human alpha1 beta2 gamma1 holo-AMPK complex bound to AMP and cyclodextrin Deposited 2014-09-23 Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 20–559（540 aa） Fragment：Human AMPK alpha1 subunit [G11-Q550]
Mutation：E471G, E474A, K476A Non-standard monomer：Yes (specific site not provided by mmCIF) STU STAUROSPORINE × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 AMP ADENOSINE MONOPHOSPHATE × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.8；293 K；12% PEG 4000,0.1 M HEPES, pH7.8, 10% 2-propanol (v/v) and 0.19 mM 7-cyclohexyl-1-heptyl-D-maltoside, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 4.05 Å R-free 0.260
4REW Crystal structure of the non-phosphorylated human alpha1 beta2 gamma1 holo-AMPK complex Deposited 2014-09-24 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 20–559（540 aa） Fragment：Human AMPK alpha1 subunit [G11-Q550]
Mutation：E471G, E474A, K476A STU STAUROSPORINE × 1 AMP ADENOSINE MONOPHOSPHATE × 3 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.8；293 K；0.1 M N-acetamido-iminodiacetic acid, pH 6.8, 9% 2-methyl-2,4-pentanediol, and 11.5 mM C-HEGA, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 4.58 Å R-free 0.259
5EZV X-ray crystal structure of AMP-activated protein kinase alpha-2/alpha-1 RIM chimaera (alpha-2(1-347)/alpha-1(349-401)/alpha-2(397-end) beta-1 gamma-1) co-crystallized with C2 (5-(5-hydroxyl-isoxazol-3-yl)-furan-2-phosphonic acid) Deposited 2015-11-26 Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 359–401（43 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) STU STAUROSPORINE × 1 C1V 3-[4-(2-hydroxyphenyl)phenyl]-4-oxidanyl-6-oxidanylidene-7H-thieno[2,3-b]pyridine-5-carbonitrile × 1 C2Z 5-(5-hydroxyl-isoxazol-3-yl)-furan-2-phosphonic acid × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；277 K；8 % PEG 3350, 0.1 M MgCl2, 1.0 % glucose, 0.001 % cocamidopropyl betaine, 0.1 M imidazole
Resolution 2.99 Å R-free 0.245
5EZV X-ray crystal structure of AMP-activated protein kinase alpha-2/alpha-1 RIM chimaera (alpha-2(1-347)/alpha-1(349-401)/alpha-2(397-end) beta-1 gamma-1) co-crystallized with C2 (5-(5-hydroxyl-isoxazol-3-yl)-furan-2-phosphonic acid) Deposited 2015-11-26 Assembly 2 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain C 359–401（43 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) STU STAUROSPORINE × 1 C1V 3-[4-(2-hydroxyphenyl)phenyl]-4-oxidanyl-6-oxidanylidene-7H-thieno[2,3-b]pyridine-5-carbonitrile × 1 C2Z 5-(5-hydroxyl-isoxazol-3-yl)-furan-2-phosphonic acid × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；277 K；8 % PEG 3350, 0.1 M MgCl2, 1.0 % glucose, 0.001 % cocamidopropyl betaine, 0.1 M imidazole
Resolution 2.99 Å R-free 0.245
6C9F AMP-activated protein kinase bound to pharmacological activator R734 Deposited 2018-01-26 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 22–480（459 aa）
Chain A 535–559（25 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) R34 5-{[6-chloro-5-(1-methyl-1H-indol-5-yl)-1H-benzimidazol-2-yl]oxy}-N-hydroxy-2-methylbenzamide × 1 STU STAUROSPORINE × 1 AMP ADENOSINE MONOPHOSPHATE × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.1 M tri-sodium acetate pH 5.6, 0.2 M ammonium acetate, 15% w/v PEG 4000
Resolution 2.92 Å R-free 0.245
6C9G AMP-activated protein kinase bound to pharmacological activator R739 Deposited 2018-01-26 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 22–480（459 aa）
Chain A 535–559（25 aa）
Mutation：S108D Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S108D Non-standard monomer：Yes (specific site not provided by mmCIF) R93 5-{[6-chloro-5-(2'-hydroxy[1,1'-biphenyl]-4-yl)-1H-benzimidazol-2-yl]oxy}-N-hydroxy-2-methylbenzamide × 1 STU STAUROSPORINE × 1 AMP ADENOSINE MONOPHOSPHATE × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.1 M tri-sodium acetate pH 5.6, 0.2 M ammonium acetate, 15% w/v PEG 4000
Resolution 2.70 Å R-free 0.240
6C9H non-phosphorylated AMP-activated protein kinase bound to pharmacological activator R734 Deposited 2018-01-26 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 22–480（459 aa）
Chain A 535–559（25 aa）
Mutation：S108D Mutation：S108D R34 5-{[6-chloro-5-(1-methyl-1H-indol-5-yl)-1H-benzimidazol-2-yl]oxy}-N-hydroxy-2-methylbenzamide × 1 STU STAUROSPORINE × 1 AMP ADENOSINE MONOPHOSPHATE × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.2 M magnesium formate
Resolution 2.65 Å R-free 0.242
6C9J AMP-activated protein kinase bound to pharmacological activator R734 Deposited 2018-01-26 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 22–480（459 aa）
Chain A 535–559（25 aa）
Mutation：S108D Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S108D Non-standard monomer：Yes (specific site not provided by mmCIF) R34 5-{[6-chloro-5-(1-methyl-1H-indol-5-yl)-1H-benzimidazol-2-yl]oxy}-N-hydroxy-2-methylbenzamide × 1 STU STAUROSPORINE × 1 AMP ADENOSINE MONOPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.1 M tri-ammonium citrate pH7, 12% w/v PEG 3350
Resolution 3.05 Å R-free 0.225
7JHG Cryo-EM structure of ATP-bound fully inactive AMPK in complex with Dorsomorphin (Compound C) and Fab-nanobody Deposited 2020-07-20 Assembly 1 Other combination Heteromer；Protein × 7 PDB declaration: heptameric（7） Consistent with protein count
Chain A 22–480（459 aa） Fragment：UNP residues 22-480,535-559
Chain A 535–559（25 aa） Fragment：UNP residues 22-480,535-559
Not recorded TAK 6-[4-(2-piperidin-1-ylethoxy)phenyl]-3-pyridin-4-ylpyrazolo[1,5-a]pyrimidine × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.47 Å
7JHH Cryo-EM structure of ATP-bound fully inactive AMPK in complex with Fab and nanobody Deposited 2020-07-20 Assembly 1 Other combination Heteromer；Protein × 7 PDB declaration: heptameric（7） Consistent with protein count
Chain A 22–480（459 aa） Fragment：UNP residues 22-480,535-559
Chain A 535–559（25 aa） Fragment：UNP residues 22-480,535-559
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.92 Å
7JIJ ATP-bound AMP-activated protein kinase Deposited 2020-07-23 Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 22–559（538 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 AMP ADENOSINE MONOPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.2 M tri-lithium citrate,10% w/v PEG3350, pH7.5,0.01 M barium chloride
Resolution 5.50 Å R-free 0.323

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.