Current Protein Identity:P02654 New Search
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
1ALE CONFORMATION OF TWO PEPTIDES CORRESPONDING TO HUMAN APOLIPOPROTEIN C-I RESIDUES 7-24 AND 35-53 IN THE PRESENCE OF SODIUM DODECYLSULFATE BY CD AND NMR SPECTROSCOPY Deposited 1995-02-20 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 33–50(18 aa)
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1ALF CONFORMATION OF TWO PEPTIDES CORRESPONDING TO HUMAN APOLIPOPROTEIN C-I RESIDUES 7-24 AND 35-53 IN THE PRESENCE OF SODIUM DODECYLSULFATE BY CD AND NMR SPECTROSCOPY Deposited 1995-02-20 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 61–79(19 aa)
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1IOJ HUMAN APOLIPOPROTEIN C-I, NMR, 18 STRUCTURES Deposited 1998-05-12 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 27–83(57 aa)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.8;323 K
NMR sample composition 5.8 mM native apoC-I, 90%H2O/10%D2O, 232 mM SDS-D25 | 90% H2O/10% D2O
NMR sample composition 5 mM selectively 15N-labeled synthetic apoC-I, 90%H2O/10%D2O, 200 mM SDS-D25 | 90% H2O/10% D2O
Resolution not provided
1OPP PEPTIDE OF HUMAN APOLIPOPROTEIN C-I RESIDUES 1-38, NMR, 28 STRUCTURES Deposited 1997-05-08 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 27–64(38 aa) Fragment:RESIDUES 1 - 38
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.8;310 K
NMR sample composition 5 mM apoC, 300 mM SDS-d2s | 90% H2O/10% D2O
NMR sample composition 5 mM apoC, 300 mM SDS-d2s | 99.9% D2O
NMR sample composition 5 mM apoC, 50 mM potassium chloride, 20 mM potassium phosphate | 50% (v/v) TFE-d, 10% D2O
Resolution not provided
6DVU Structure of the Monoclinic-1 (Monocl-1) Crystal Form of Human Apolipoprotein C1 Deposited 2018-06-25 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–83(83 aa)
Chain B 1–83(83 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 8;298 K;Crystallized in Cryschem sitting drop plates with reservoirs of 16%-18% 2-methyl-2,4-pentanediol (MPD), 0.1 M sodium acetate and 0.25% octyl-beta-s-1-thioglucopyanoside. The drops were composed of equal amounts of 8 mg/ml protein in 0.02 ammonium bicarbonate and reservoir.
Resolution 1.80 Å R-free 0.276
6DXR Structure of the Monoclinic-2 (Monocl-2) Crystal Form of Human Apolipoprotein C1 Deposited 2018-06-29 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–83(83 aa)
Chain B 1–83(83 aa)
Not recorded MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 6;298 K;20% PEG
Resolution 2.00 Å R-free 0.287
6DZ6 Structure of the Orthorhombic (Orthrhmb) Crystal Form of Human Apolipoprotein C1 Deposited 2018-07-03 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–83(83 aa)
Chain B 1–83(83 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION;pH 6;298 K;16% MPD - 18% MPD
Resolution 3.00 Å R-free 0.283
6NF3 Structure of the Monoclinic-3 (Monocln-3) Crystal Form of Human Apolipoprotein C1 Deposited 2018-12-18 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–83(83 aa)
Chain B 1–83(83 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION;pH 6.5;298 K;The crystals were grown by sitting drop vapor diffusion in Cryschem plates using 0.6 ml reservoirs of 16% to 18% 2-methyl-2,4-pentanediol (MPD) containing o.1 M sodium acetate and 0.25% octyl-beta-s-1-thioglucopyanoside. The drops were equal volumes, generally 6 ul each, of the reservoir and an 8 mg/ml solution of protein dissolved in .02 M ammonium bicarbonate.
Resolution 2.33 Å R-free 0.318