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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：Q9UIC8 New Search
3PDB entries
10Biological assembly
10chain/assembly records
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
3IEI Crystal structure of human leucine carboxylmethyltransferase-1 in complex with S-adenosyl homocysteine Deposited 2009-07-22 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1–334（334 aa）
Mutation：C19M, A21E, D22N, P115S SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；Protein solution (10 mg/ml LCMT-1, 5 mM SAH) was mixed with an equal volume of reservoir solution containing 17-19% v/v PEG MME 2000, 150 mM Triethylamine N-oxide, 5 mM DTT, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.90 Å R-free 0.232
3IEI Crystal structure of human leucine carboxylmethyltransferase-1 in complex with S-adenosyl homocysteine Deposited 2009-07-22 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 1–334（334 aa）
Mutation：C19M, A21E, D22N, P115S SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 GOL GLYCEROL × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；Protein solution (10 mg/ml LCMT-1, 5 mM SAH) was mixed with an equal volume of reservoir solution containing 17-19% v/v PEG MME 2000, 150 mM Triethylamine N-oxide, 5 mM DTT, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.90 Å R-free 0.232
3IEI Crystal structure of human leucine carboxylmethyltransferase-1 in complex with S-adenosyl homocysteine Deposited 2009-07-22 Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain C 1–334（334 aa）
Mutation：C19M, A21E, D22N, P115S SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；Protein solution (10 mg/ml LCMT-1, 5 mM SAH) was mixed with an equal volume of reservoir solution containing 17-19% v/v PEG MME 2000, 150 mM Triethylamine N-oxide, 5 mM DTT, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.90 Å R-free 0.232
3IEI Crystal structure of human leucine carboxylmethyltransferase-1 in complex with S-adenosyl homocysteine Deposited 2009-07-22 Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain D 1–334（334 aa）
Mutation：C19M, A21E, D22N, P115S SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 GOL GLYCEROL × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；Protein solution (10 mg/ml LCMT-1, 5 mM SAH) was mixed with an equal volume of reservoir solution containing 17-19% v/v PEG MME 2000, 150 mM Triethylamine N-oxide, 5 mM DTT, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.90 Å R-free 0.232
3IEI Crystal structure of human leucine carboxylmethyltransferase-1 in complex with S-adenosyl homocysteine Deposited 2009-07-22 Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain E 1–334（334 aa）
Mutation：C19M, A21E, D22N, P115S SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 GOL GLYCEROL × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；Protein solution (10 mg/ml LCMT-1, 5 mM SAH) was mixed with an equal volume of reservoir solution containing 17-19% v/v PEG MME 2000, 150 mM Triethylamine N-oxide, 5 mM DTT, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.90 Å R-free 0.232
3IEI Crystal structure of human leucine carboxylmethyltransferase-1 in complex with S-adenosyl homocysteine Deposited 2009-07-22 Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain F 1–334（334 aa）
Mutation：C19M, A21E, D22N, P115S SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；Protein solution (10 mg/ml LCMT-1, 5 mM SAH) was mixed with an equal volume of reservoir solution containing 17-19% v/v PEG MME 2000, 150 mM Triethylamine N-oxide, 5 mM DTT, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.90 Å R-free 0.232
3IEI Crystal structure of human leucine carboxylmethyltransferase-1 in complex with S-adenosyl homocysteine Deposited 2009-07-22 Assembly 7 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain G 1–334（334 aa）
Mutation：C19M, A21E, D22N, P115S SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；Protein solution (10 mg/ml LCMT-1, 5 mM SAH) was mixed with an equal volume of reservoir solution containing 17-19% v/v PEG MME 2000, 150 mM Triethylamine N-oxide, 5 mM DTT, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.90 Å R-free 0.232
3IEI Crystal structure of human leucine carboxylmethyltransferase-1 in complex with S-adenosyl homocysteine Deposited 2009-07-22 Assembly 8 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain H 1–334（334 aa）
Mutation：C19M, A21E, D22N, P115S SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 GOL GLYCEROL × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；Protein solution (10 mg/ml LCMT-1, 5 mM SAH) was mixed with an equal volume of reservoir solution containing 17-19% v/v PEG MME 2000, 150 mM Triethylamine N-oxide, 5 mM DTT, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.90 Å R-free 0.232
3O7W The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1 Deposited 2010-08-01 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 23–334（312 aa） Fragment：UNP residues 23-334 with deletion of residues 233-258
Not recorded GOL GLYCEROL × 1 SAM S-ADENOSYLMETHIONINE × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；295 K；0.05 M Ammonium Sulfate, 0.05M Bis Tris (pH6.5), 30% Pentaerythritol Ethoxylate, VAPOR DIFFUSION, SITTING DROP, temperature 295K
Resolution 2.00 Å R-free 0.265
3P71 Crystal structure of the complex of LCMT-1 and PP2A Deposited 2010-10-11 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain T 1–334（334 aa）
Mutation：C19M, A21E, D22N, P115S PEG DI(HYDROXYETHYL)ETHER × 1 AN6 5'-{[(3S)-3-amino-3-carboxypropyl](ethyl)amino}-5'-deoxyadenosine × 1 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.2；291 K；PROTEIN COMPLEX (~5 MG/ML), 100MM TRIS-HCL, 22-26% V/V PEG 4000, 200 MM SODIUM ACETATE, 5 MM DTT, pH 8.2, VAPOR DIFFUSION, SITTING DROP, temperature 291K
Resolution 2.70 Å R-free 0.249

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.