Current Protein Identity:A0A1W2PRB0 New Search
Main Difference Dimensions in This Set
Different mutation/modification Different assembly state Different ligand/ion 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
7YNZ Cryo-EM structure of human Slo1-LRRC26 complex with C1 symmetry Deposited 2022-08-01 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
Chain A 66–1125(1060 aa)
Chain C 66–1125(1060 aa)
Chain E 66–1125(1060 aa)
Chain G 66–1125(1060 aa)
Mutation:K577S Mutation:K577S Mutation:K577S Mutation:K577S MG MAGNESIUM ION × 4 CA CALCIUM ION × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å
7YO0 Cryo-EM structure of human Slo1-LRRC26 complex with Symmetry Expansion Deposited 2022-08-01 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
Chain A 66–1125(1060 aa)
Chain C 66–1125(1060 aa)
Chain E 66–1125(1060 aa)
Chain G 66–1125(1060 aa)
Mutation:K577S Mutation:K577S Mutation:K577S Mutation:K577S PGW (1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate × 4 MG MAGNESIUM ION × 4 CA CALCIUM ION × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
7YO1 Cryo-EM structure of RCK1 mutated human Slo1-LRRC26 complex Deposited 2022-08-01 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
Chain A 66–1125(1060 aa)
Chain C 66–1125(1060 aa)
Chain E 66–1125(1060 aa)
Chain G 66–1125(1060 aa)
Mutation:D372A, D367A, K577S Mutation:D372A, D367A, K577S Mutation:D372A, D367A, K577S Mutation:D372A, D367A, K577S MG MAGNESIUM ION × 4 CA CALCIUM ION × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
7YO2 Cryo-EM structure of RCK1-RCK2 mutated human Slo1 apo Deposited 2022-08-01 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 66–1125(1060 aa)
Chain B 66–1125(1060 aa)
Chain C 66–1125(1060 aa)
Chain D 66–1125(1060 aa)
Mutation:D362A, D367A, D894N, D895N, D896N, D897N, D898N Mutation:D362A, D367A, D894N, D895N, D896N, D897N, D898N Mutation:D362A, D367A, D894N, D895N, D896N, D897N, D898N Mutation:D362A, D367A, D894N, D895N, D896N, D897N, D898N No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
7YO3 Cryo-EM structure of human Slo1-LRRC26 complex with C4 symmetry Deposited 2022-08-01 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 66–1125(1060 aa)
Mutation:K577S MG MAGNESIUM ION × 1 CA CALCIUM ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å
7YO4 Cryo-EM structure of RCK1-RCK2 mutated human Slo1-LRRC26 complex Deposited 2022-08-01 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
Chain A 66–1125(1060 aa)
Chain C 66–1125(1060 aa)
Chain E 66–1125(1060 aa)
Chain G 66–1125(1060 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.90 Å
7YO5 Cryo-EM structure of RCK1 mutated human Slo1 apo Deposited 2022-08-01 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 66–1125(1060 aa)
Chain B 66–1125(1060 aa)
Chain C 66–1125(1060 aa)
Chain D 66–1125(1060 aa)
Mutation:D362A, D367A, K577S Mutation:D362A, D367A, K577S Mutation:D362A, D367A, K577S Mutation:D362A, D367A, K577S CA CALCIUM ION × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.90 Å