Current Protein Identity:P28562
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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 |
|---|---|---|---|---|---|---|---|
| 6APX Crystal structure of human dual specificity phosphatase 1 catalytic domain (C258S) as a maltose binding protein fusion in complex with the monobody YSX1 Deposited 2017-08-18 | Assembly 1 Insufficient information Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain A
172–314(143 aa)
|
Mutation:D82A, K83A, E172A, N173A, K239A, K362A, E359A, D363A, C258S | SO4 SULFATE ION × 3 GOL GLYCEROL × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 5.9;292 K;75 mM MES pH 5.9
2.4 M ammonium sulfate
|
Resolution 2.49 Å R-free 0.236 |
| 6D65 Crystal structure of the human dual specificity phosphatase 1 catalytic domain (C258S) as a maltose binding protein fusion in complex with the designed AR protein off7 Deposited 2018-04-20 | Assembly 1 Insufficient information Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain A
172–314(143 aa)
|
Mutation:D82A, K83A, E172A, N173A, K239A, E362A, D363A, C258S | GOL GLYCEROL × 4 SO4 SULFATE ION × 11 EOH ETHANOL × 9 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 6;292 K;0.15 M NaCl
0.1 M sodium cacodylate
2.0 M ammonium sulfate
|
Resolution 2.35 Å R-free 0.241 |
| 6D65 Crystal structure of the human dual specificity phosphatase 1 catalytic domain (C258S) as a maltose binding protein fusion in complex with the designed AR protein off7 Deposited 2018-04-20 | Assembly 2 Insufficient information Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain C
172–314(143 aa)
|
Mutation:D82A, K83A, E172A, N173A, K239A, E362A, D363A, C258S | GOL GLYCEROL × 2 SO4 SULFATE ION × 12 EOH ETHANOL × 12 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 6;292 K;0.15 M NaCl
0.1 M sodium cacodylate
2.0 M ammonium sulfate
|
Resolution 2.35 Å R-free 0.241 |
| 6D66 Crystal structure of the human dual specificity 1 catalytic domain (C258S) as a maltose binding protein fusion in complex with the designed AR protein mbp3_16 Deposited 2018-04-20 | Assembly 1 Insufficient information Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain A
172–314(143 aa)
|
Mutation:D82A, K83A, E172A, N173A, K239A, E362A, D363A, C258S,D82A, K83A, E172A, N173A, K239A, E362A, D363A, C258S | PEG DI(HYDROXYETHYL)ETHER × 3 PO4 PHOSPHATE ION × 1 GLY GLYCINE × 3 PGE TRIETHYLENE GLYCOL × 3 EDO 1,2-ETHANEDIOL × 12 PG4 TETRAETHYLENE GLYCOL × 1 DAL D-ALANINE × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 8.5;292 K;0.2 M DL-glutamic acid
0.2 M DL-alanine
0.2 M -glycine
0.2 M-DL-lysine
0.2 M DL-serine
0.1 M Tris: Bicine
25% MPD
25% PEG1000
25% PEG3350
|
Resolution 2.23 Å R-free 0.202 |
| 6D67 Crystal structure of the human dual specificity phosphatase 1 catalytic domain (C258S) as a maltose binding protein fusion (maltose bound form) in complex with the designed AR protein mbp3_16 Deposited 2018-04-20 | Assembly 1 Insufficient information Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain A
172–314(143 aa)
|
Mutation:D82A, K83A, E172A, N173A, K239A, E359A, K362A, D363A,D82A, K83A, E172A, N173A, C258S, K239A, E359A, K362A, D363A | PEG DI(HYDROXYETHYL)ETHER × 1 PO4 PHOSPHATE ION × 1 EDO 1,2-ETHANEDIOL × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 8.5;292 K;0.2 M DL-GLUTAMIC ACID
0.2 M DL-ALANINE
0.2 M GLYCINE
0.2 M DL-LYSINE
0.2 M DL-SERINE
0.1 M TRIS; BICINE
25% MPD
25% PEG1000
25% PEG3350
|
Resolution 2.55 Å R-free 0.252 |