Current Protein Identity:P04745 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion 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
1C8Q STRUCTURE SOLUTION AND REFINEMENT OF THE RECOMBINANT HUMAN SALIVARY AMYLASE Deposited 2000-06-08 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 16–511(496 aa)
Non-standard monomer:Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 9;273 K;10 mM Tris- HCL containing 5 mM CaCl2, 44% MPD, protein concentration 20 mg/ml, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 273K
Resolution 2.30 Å R-free 0.216
1JXJ Role of mobile loop in the mechanism of human salivary amylase Deposited 2001-09-07 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 16–511(496 aa)
Mutation:W58L Non-standard monomer:Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 9;298 K;MPD, calcium chloride, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K, temperature 298.0K
Resolution 1.99 Å R-free 0.198
1JXK Role of ethe mobile loop in the mehanism of human salivary amylase Deposited 2001-09-07 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 16–511(496 aa) Fragment:lacking the loop residues 306-310
Non-standard monomer:Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 9;298 K;MPD, calcium chloride, pH 9.0, VAPOR DIFFUSION, HANGING DROP at 298K
Resolution 1.90 Å R-free 0.200
1MFU Probing the role of a mobile loop in human salivary amylase: Structural studies on the loop-deleted mutant Deposited 2002-08-13 Assembly 1 Other combination Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 17–511(495 aa)
Mutation:deletion of residues 306 through 310 Non-standard monomer:Yes (specific site not provided by mmCIF) HMC 5-HYDROXYMETHYL-CHONDURITOL × 4 GLC alpha-D-glucopyranose × 1 CA CALCIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions soaking with acarbose at 1 mM concentration for 24 hours;pH 9;298 K;40% mpd, pH 9.0, soaking with acarbose at 1 mM concentration for 24 hours, temperature 298K
Resolution 2.00 Å R-free 0.201
1MFV Probing the role of a mobile loop in human slaivary amylase: Structural studies on the loop-deleted enzyme Deposited 2002-08-13 Assembly 1 Other combination Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 17–511(495 aa)
Non-standard monomer:Yes (specific site not provided by mmCIF) HMC 5-HYDROXYMETHYL-CHONDURITOL × 2 CA CALCIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions vapordiffusion, combined with soaking with inhibitor at 1 mM concentration;pH 9;298 K;40% MPD, pH 9.0, vapordiffusion, combined with soaking with inhibitor at 1 mM concentration, temperature 298K
Resolution 2.00 Å R-free 0.195
1NM9 Crystal structure of recombinant human salivary amylase mutant W58A Deposited 2003-01-09 Assembly 1 Other combination Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 16–511(496 aa)
Mutation:W58A Non-standard monomer:Yes (specific site not provided by mmCIF) HMC 5-HYDROXYMETHYL-CHONDURITOL × 1 GLC alpha-D-glucopyranose × 1 CA CALCIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 9;323 K;MPD, Calcium chloride, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 323K
Resolution 2.10 Å R-free 0.196
1Q4N Structural studies of Phe256Trp of human salivary alpha-amylase: implications for the role of a conserved water molecule and its associated chain in enzyme activity Deposited 2003-08-04 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain X 16–511(496 aa)
Mutation:F256W Non-standard monomer:Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 CL CHLORIDE ION × 1 TAM TRIS(HYDROXYETHYL)AMINOMETHANE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 9;MPD, Calcium Chloride, Tris, pH 9.00, VAPOR DIFFUSION, HANGING DROP, temperature 100K
Resolution 2.07 Å R-free 0.206
1SMD HUMAN SALIVARY AMYLASE Deposited 1996-01-24 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 17–511(495 aa)
Non-standard monomer:Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.60 Å
1XV8 Crystal Structure of Human Salivary Alpha-Amylase Dimer Deposited 2004-10-27 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 16–511(496 aa) Fragment:HSA
Chain B 16–511(496 aa) Fragment:HSA
Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) CA CALCIUM ION × 2 CL CHLORIDE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6.5;0.2 M Ca acetate, 0.1 M Na cacodylate (pH 6.5), 18% PEG 8K, VAPOR DIFFUSION, HANGING DROP, temperature 100K
Resolution 3.00 Å R-free 0.271
1Z32 Structure-function relationships in human salivary alpha-amylase: Role of aromatic residues Deposited 2005-03-10 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain X 16–511(496 aa)
Mutation:Y151M Non-standard monomer:Yes (specific site not provided by mmCIF) GLC alpha-D-glucopyranose × 1 AGL 4-amino-4,6-dideoxy-alpha-D-glucopyranose × 1 HMC 5-HYDROXYMETHYL-CHONDURITOL × 1 CA CALCIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 9;MPD 40%, pH 9.0, VAPOR DIFFUSION, HANGING DROP
Resolution 1.60 Å R-free 0.192
3BLK Role of aromatic residues in starch binding Deposited 2007-12-11 Assembly 1 Other combination Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 16–511(496 aa)
Mutation:W316A Non-standard monomer:Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 CL CHLORIDE ION × 1 HMC 5-HYDROXYMETHYL-CHONDURITOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 9;298 K;45% MPD, 0.1M Tris.HCl, 10 mM calcium chloride, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.00 Å R-free 0.215
3BLP Role of aromatic residues in human salivary alpha-amylase Deposited 2007-12-11 Assembly 1 Other combination Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain X 16–511(496 aa)
Mutation:W388A Non-standard monomer:Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 CL CHLORIDE ION × 1 HMC 5-HYDROXYMETHYL-CHONDURITOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 9;298 K;45% MPD, 0.1M Tris.HCl, 10 mM calcium chloride, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.60 Å R-free 0.205
3DHP Probing the role of aromatic residues at the secondary saccharide binding sites of human salivary alpha-amylase in substrate hydrolysis and bacterial binding Deposited 2008-06-18 Assembly 1 Other combination Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 16–511(496 aa)
Mutation:W134A,W203A,Y276A,W284A,W316A,W388A Non-standard monomer:Yes (specific site not provided by mmCIF) GLC alpha-D-glucopyranose × 1 CA CALCIUM ION × 1 CL CHLORIDE ION × 1 HMC 5-HYDROXYMETHYL-CHONDURITOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions hanging drop;pH 9;298 K;MPD, pH 9.0, hanging drop, temperature 298K
Resolution 1.50 Å R-free 0.186