Current Protein Identity:P14151 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
2LGF Solution structure of Ca2+/calmodulin complexed with a peptide representing the calmodulin-binding domain of L-selectin Deposited 2011-07-25 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 349–363(15 aa) Fragment:sequence database residues 349-363
Not recorded CA CALCIUM ION × 4 SOLUTION NMR
NMR measurement conditions pH 6.8;303 K;Ionic strength (raw mmCIF value) 0.1;Pressure ambient
NMR measurement conditions pH 6.8;303 K;Ionic strength (raw mmCIF value) 0.3;Pressure ambient
NMR sample composition 0.5-0.8 mM [U-13C; U-15N] protein_1, 0.5-0.8 mM protein_2, 4 mM CALCIUM ION, 0.5 mM DSS, 100 mM potassium chloride, 0.03 % sodium azide, 20 mM Bis-Tris, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5-0.8 mM [U-2H; U-15N] protein_1, 0.5-0.8 mM protein_2, 4 mM CALCIUM ION, 0.5 mM DSS, 100 mM potassium chloride, 0.03 % sodium azide, 20 mM Bis-Tris, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5-0.8 mM [1H/13C-methyl Met; U-2H; U-15N] protein_1, 0.5-0.8 mM protein_2, 4 mM CALCIUM ION, 0.5 mM DSS, 100 mM potassium chloride, 0.03 % sodium azide, 20 mM Bis-Tris, 100% D2O | 100% D2O
NMR sample composition 0.5-0.8 mM [U-13C; U-15N] protein_1, 0.5-0.8 mM protein_2, 4 mM CALCIUM ION, 0.5 mM DSS, 300 mM potassium chloride, 0.03 % sodium azide, 20 mM Bis-Tris, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5-0.8 mM [U-13C; U-15N] protein_1, 0.5-0.8 mM protein_2, 4 mM CALCIUM ION, 0.5 mM DSS, 300 mM potassium chloride, 0.03 % sodium azide, 20 mM Bis-Tris, 16 w/v Pf1 phage, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
3CFW L-selectin lectin and EGF domains Deposited 2008-03-04 Assembly 1 Other combination Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 39–194(156 aa) Fragment:EGF domain (UNP residues 39-194)
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;0.17 M Sodium acetate trihydrate, 0.085 M Tris-HCl, pH 8.5, 25.5 % w/v PEG 4000,15% v/v Glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.20 Å R-free 0.248
5VC1 Crystal structure of L-selectin lectin/EGF domains Deposited 2017-03-30 Assembly 1 Other combination Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 39–195(157 aa) Fragment:UNP residues 39-195
Mutation:N22Q, N139Q PG4 TETRAETHYLENE GLYCOL × 1 PEG DI(HYDROXYETHYL)ETHER × 1 GOL GLYCEROL × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;100 mM sodium cacodylate pH 7.5, 200 mM calcium acetate, 40% (v/v) PEG 600
Resolution 1.94 Å R-free 0.231