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1ura

ALKALINE PHOSPHATASE (D51ZN)

Method: X-RAY DIFFRACTION Dmax: 99.6 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ALKALINE PHOSPHATASE

Escherichia coli

UniProt P00634

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 26–471 Chain B； UniProt 26–471 Mutation：D51N ZN ZINC ION × 4 PO4 PHOSPHATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；65% SATURATING (NH4)2SO4, 100 MM TRIS, 10 MM MGCL2, 10 MM ZNCL2, 2 MM NAH2PO4 AT PH 7.5. Resolution 2.04 Å R-free 0.234

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 1URA Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1AJA THREE-DIMENSIONAL STRUCTURE OF THE D153G MUTANT OF E. COLI ALKALINE PHOSPHATASE: A MUTANT WITH WEAKER MAGNESIUM BINDING AND INCREASED CATALYTIC ACTIVITY Deposited 1995-08-19 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：D153G Mutation：D153G No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.50 Å
1AJB THREE-DIMENSIONAL STRUCTURE OF THE D153G MUTANT OF E. COLI ALKALINE PHOSPHATASE: A MUTANT WITH WEAKER MAGNESIUM BINDING AND INCREASED CATALYTIC ACTIVITY Deposited 1995-08-19 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：D153G Mutation：D153G ZN ZINC ION × 4 MG MAGNESIUM ION × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.50 Å
1AJC THREE-DIMENSIONAL STRUCTURE OF THE D153G MUTANT OF E. COLI ALKALINE PHOSPHATASE: A MUTANT WITH WEAKER MAGNESIUM BINDING AND INCREASED CATALYTIC ACTIVITY Deposited 1995-07-18 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：D153G Mutation：D153G ZN ZINC ION × 4 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.50 Å
1AJD THREE-DIMENSIONAL STRUCTURE OF THE D153G MUTANT OF E. COLI ALKALINE PHOSPHATASE: A MUTANT WITH WEAKER MAGNESIUM BINDING AND INCREASED CATALYTIC ACTIVITY Deposited 1995-08-18 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：D153G Mutation：D153G ZN ZINC ION × 4 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.50 Å
1ALH KINETICS AND CRYSTAL STRUCTURE OF A MUTANT E. COLI ALKALINE PHOSPHATASE (ASP-369-->ASN): A MECHANISM INVOLVING ONE ZINC PER ACTIVE SITE Deposited 1994-08-23 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 26–471（446 aa）
Chain B 26–471（446 aa）
Not recorded ZN ZINC ION × 2 PO4 PHOSPHATE ION × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.50 Å
1ALI ALKALINE PHOSPHATASE MUTANT (H412N) Deposited 1995-06-02 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：H412N Mutation：H412N ZN ZINC ION × 4 MG MAGNESIUM ION × 2 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions THE STRUCTURE IS OF A MUTANT ALKALINE PHOSPHATE (H412N) IN WHICH HIS 412 IS REPLACED BY ASN, DETERMINED WITH CRYSTALS SOAKED IN STABILIZATION BUFFER CONTAINING 10 MM ZINC CHLORIDE. THERE ARE TWO ZINCS AND ONE MAGNESIUM COMPLEXED WITH AN INORGANIC PHOSPHATE BOUND IN EACH OF THE TWO ACTIVE SITES.
Resolution 2.20 Å
1ALJ ALKALINE PHOSPHATASE MUTANT (H412N) Deposited 1995-06-02 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：H412N Mutation：H412N ZN ZINC ION × 2 MG MAGNESIUM ION × 2 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions THIS ENTRY IS A MUTANT ALKALINE PHOSPHATE (H412N) IN WHICH HIS 412 IS REPLACED BY ASN, DETERMINED WITH CRYSTALS SOAKED IN STABILIZATION BUFFER CONTAINING NO ADDED ZINC. THERE IS ONE ZINC AND ONE MAGNESIUM COMPLEXED WITH INORGANIC PHOSPHATE BOUND IN EACH OF THE TWO ACTIVE SITES.
Resolution 2.60 Å
1ALK REACTION MECHANISM OF ALKALINE PHOSPHATASE BASED ON CRYSTAL STRUCTURES. TWO METAL ION CATALYSIS Deposited 1993-03-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Not recorded ZN ZINC ION × 4 MG MAGNESIUM ION × 2 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
1ANI ALKALINE PHOSPHATASE (D153H, K328H) Deposited 1995-09-06 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 26–471（446 aa）
Chain B 26–471（446 aa）
Mutation：D153H, K328H Mutation：D153H, K328H ZN ZINC ION × 6 PO4 PHOSPHATE ION × 5 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；pH 7.5
Resolution 2.50 Å
1ANJ ALKALINE PHOSPHATASE (K328H) Deposited 1995-09-06 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 26–471（446 aa）
Chain B 26–471（446 aa）
Mutation：K328H Mutation：K328H ZN ZINC ION × 6 PO4 PHOSPHATE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；pH 7.5
Resolution 2.30 Å R-free 0.249
1B8J ALKALINE PHOSPHATASE COMPLEXED WITH VANADATE Deposited 1999-02-01 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 4 SO4 SULFATE ION × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；CRYSTALLIZATION CONDITIONS: 65 % SATURATING (NH4)2SO4, 100 MM TRIS, 10 MM MGCL2, 1 MM ZNCL2, 0.1 MM NH4VO3, PH 7.5
Resolution 1.90 Å R-free 0.196
1ED8 STRUCTURE OF E. COLI ALKALINE PHOSPHATASE INHIBITED BY THE INORGANIC PHOSPHATE AT 1.75A RESOLUTION Deposited 2000-01-27 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Not recorded ZN ZINC ION × 6 MG MAGNESIUM ION × 2 PO4 PHOSPHATE ION × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；Tris, ammonium sulfate, magnesium chloride, zinc chloride , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 1.75 Å R-free 0.228
1ED9 STRUCTURE OF E. COLI ALKALINE PHOSPHATASE WITHOUT THE INORGANIC PHOSPHATE AT 1.75A RESOLUTION Deposited 2000-01-27 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Not recorded ZN ZINC ION × 4 MG MAGNESIUM ION × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；Tris, ammonium sulfate, magnesium chloride, zinc chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 1.75 Å R-free 0.224
1ELX E. COLI ALKALINE PHOSPHATASE MUTANT (S102A) Deposited 1998-02-10 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：S102A Mutation：S102A ZN ZINC ION × 4 MG MAGNESIUM ION × 2 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；25 MG/ML PROTEIN IN 39% SATURATING (NH4)2SO4, 100 MM TRIS, 10 MM MGCL2 100 MM ZNCL2, 2 MM NAH2PO4 AT PH 7.5, EQUILIBRATED AGAINST 55% SATURATING (NH4)2SO4
Resolution 2.60 Å R-free 0.207
1ELY E. COLI ALKALINE PHOSPHATASE MUTANT (S102C) Deposited 1998-02-10 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：S102C Mutation：S102C ZN ZINC ION × 4 MG MAGNESIUM ION × 2 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；25 MG/ML PROTEIN IN 39% SATURATING (NH4)2SO4, 100 MM TRIS, 10 MM MGCL2 100 MM ZNCL2, 2 MM NAH2PO4 AT PH 7.5, EQUILIBRATED AGAINST 55% SATURATING (NH4)2SO4
Resolution 2.80 Å R-free 0.193
1ELZ E. COLI ALKALINE PHOSPHATASE MUTANT (S102G) Deposited 1998-02-10 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：S102G Mutation：S102G ZN ZINC ION × 4 MG MAGNESIUM ION × 2 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；25 MG/ML PROTEIN IN 39% SATURATING (NH4)2SO4, 100 MM TRIS, 10 MM MGCL2 100 MM ZNCL2, 2 MM NAH2PO4 AT PH 7.5, EQUILIBRATED AGAINST 55% SATURATING (NH4)2SO4
Resolution 2.80 Å R-free 0.173
1EW8 ALKALINE PHOSPHATASE (E.C. 3.1.3.1) COMPLEX WITH PHOSPHONOACETIC ACID Deposited 2000-04-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Not recorded ZN ZINC ION × 6 PO4 PHOSPHATE ION × 2 SO4 SULFATE ION × 2 MG MAGNESIUM ION × 2 PAE PHOSPHONOACETIC ACID × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.5；298 K；enzyme: 30 mg/mL; buffer: 40% saturating ammonium sulfate/100 mM Tris/10 mM MgSO4, pH 9.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.20 Å R-free 0.257
1EW9 ALKALINE PHOSPHATASE (E.C. 3.1.3.1) COMPLEX WITH MERCAPTOMETHYL PHOSPHONATE Deposited 2000-04-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Not recorded ZN ZINC ION × 6 SO4 SULFATE ION × 2 MG MAGNESIUM ION × 2 MMQ MERCAPTOMETHYL PHOSPHONATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.5；298 K；enzyme: 30 mg/mL; buffer: 40% saturated ammonium sulfate, 100 mM Tris/10 mM magnesium sulfate, pH 9.5, VAPOR DIFFUSION, HANGING DROP, temperature 25K
Resolution 2.00 Å R-free 0.229
1HJK ALKALINE PHOSPHATASE MUTANT H331Q Deposited 1997-05-30 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：H331Q Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：H331Q Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 4 MG MAGNESIUM ION × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；55% SATURATING (NH4)2SO4, 100 MM TRIS, 10 MM MGCL2, 10 MM ZNCL2, 2 MM NAH2PO4 AT PH 7.5
Resolution 2.30 Å R-free 0.200
1HQA ALKALINE PHOSPHATASE (H412Q) Deposited 1995-11-30 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：H412Q Mutation：H412Q ZN ZINC ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；pH 7.5
Resolution 2.25 Å
1KH4 E. COLI ALKALINE PHOSPHATASE MUTANT (D330N) IN COMPLEX WITH PHOSPHATE Deposited 2001-11-29 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：D330N Mutation：D330N ZN ZINC ION × 4 MG MAGNESIUM ION × 2 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；Ammonium sulfate, magnesium chloride, zinc sulfate, TRIS, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.40 Å R-free 0.245
1KH5 E. COLI ALKALINE PHOSPHATASE MUTANT (D330N) MIMIC OF THE TRANSITION STATES WITH ALUMINIUM FLUORIDE Deposited 2001-11-29 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：D330N Mutation：D330N ZN ZINC ION × 4 MG MAGNESIUM ION × 2 AF3 ALUMINUM FLUORIDE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；292 K；Ammonium sulfate, magnesium chloride, zinc sulfate, TRIS, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K
Resolution 2.00 Å R-free 0.228
1KH7 E. COLI ALKALINE PHOSPHATASE MUTANT (D153GD330N) Deposited 2001-11-29 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：D153G, D330N Mutation：D153G, D330N ZN ZINC ION × 4 MG MAGNESIUM ION × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；292 K；ammonium sulfate, magnesium chloride, zinc sulfate, TRIS, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K
Resolution 2.40 Å R-free 0.249
1KH9 E. COLI ALKALINE PHOSPHATASE MUTANT (D153GD330N) COMPLEX WITH PHOSPHATE Deposited 2001-11-29 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：D153G, D330N Mutation：D153G, D330N ZN ZINC ION × 4 MG MAGNESIUM ION × 1 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；292 K；ammonium sulfate, magnesium chloride, zinc sulfate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K
Resolution 2.50 Å R-free 0.250
1KHJ E. COLI ALKALINE PHOSPHATASE MUTANT (D153HD330N) MIMIC OF THE TRANSITION STATES WITH ALUMINIUM FLUORIDE Deposited 2001-11-30 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：D153H, D330N Mutation：D153H, D330N ZN ZINC ION × 4 AF3 ALUMINUM FLUORIDE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；292 K；ammonium sulfate, magnesium chloride, zinc sulfate, TRIS, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K
Resolution 2.30 Å R-free 0.223
1KHK E. COLI ALKALINE PHOSPHATASE MUTANT (D153HD330N) Deposited 2001-11-30 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：D153H, D330N Mutation：D153H, D330N ZN ZINC ION × 4 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；292 K；ammonium sulfate, magnesium chloride, zinc sulfate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K
Resolution 2.50 Å R-free 0.207
1KHL E. COLI ALKALINE PHOSPHATASE MUTANT (D153HD330N) COMPLEX WITH PHOSPHATE Deposited 2001-11-30 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：D153H, D330N Mutation：D153H, D330N ZN ZINC ION × 4 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；292 K；ammonium sulfate, magnesium chloride, zinc sulfate, TRIS, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K
Resolution 2.50 Å R-free 0.227
1KHN E. COLI ALKALINE PHOSPHATASE MUTANT (D153HD330N) ZINC FORM Deposited 2001-11-30 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：D153H, D330N Mutation：D153H, D330N ZN ZINC ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；292 K；ammonium sulfate, magnesium chloride, zinc sulfate, TRIS, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K
Resolution 2.60 Å R-free 0.248
1URB ALKALINE PHOSPHATASE (N51MG) Deposited 1996-02-03 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 26–471（446 aa）
Chain B 26–471（446 aa）
Mutation：D51N Mutation：D51N ZN ZINC ION × 2 MG MAGNESIUM ION × 2 PO4 PHOSPHATE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 9.2；45% SATURATING (NH4)2SO4, 0.10 MM CAPS, 20 MM MGCL2, 10 UM ZNCL2, 0.1 MM NAH2PO4 AT PH 9.2.
Resolution 2.14 Å R-free 0.241
1Y6V Structure of E. coli Alkaline Phosphatase in presence of cobalt at 1.60 A resolution Deposited 2004-12-07 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Not recorded CO COBALT (II) ION × 6 PO4 PHOSPHATE ION × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.5；293 K；10 mM cobalt chloride, 2.1 M Ammonium sulfate, pH 9.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.60 Å R-free 0.212
1Y7A Structure of D153H/K328W E. coli alkaline phosphatase in presence of cobalt at 1.77 A resolution Deposited 2004-12-08 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：D153H, K328W Mutation：D153H, K328W CO COBALT (II) ION × 6 PO4 PHOSPHATE ION × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.5；293 K；10 mM cobalt chloride, 2.2 M ammonium sulfate, pH 9.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.77 Å R-free 0.238
2ANH ALKALINE PHOSPHATASE (D153H) Deposited 1995-09-06 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 26–471（446 aa）
Chain B 26–471（446 aa）
Mutation：D153H Mutation：D153H ZN ZINC ION × 6 PO4 PHOSPHATE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；pH 7.5
Resolution 2.40 Å R-free 0.239
2G9Y Structure of S102T E. coli alkaline phosphatase in presence of phosphate at 2.00 A resolution Deposited 2006-03-07 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：S102T Mutation：S102T ZN ZINC ION × 4 MG MAGNESIUM ION × 2 PO4 PHOSPHATE ION × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.5；293 K；2.0M ammonium sulfate, 100mM Tris, 10mM magnesium chloride, 0.01mM zinc chloride, pH 9.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.00 Å R-free 0.242
2GA3 Structure of S102T E. coli Alkaline Phosphatase-phosphate intermediate at 2.20A resolution Deposited 2006-03-07 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：S102(TPO) Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S102(TPO) Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 4 MG MAGNESIUM ION × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.5；293 K；2.0M ammonium sulfate, 100mM Tris, 10mM magnesium chloride, 0.01mM zinc chloride, pH 9.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.20 Å R-free 0.229
2MLZ NMR structure of E. coli Trigger Factor in complex with unfolded PhoA365-471 Deposited 2014-03-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 360–471（112 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；295 K；Ionic strength (raw mmCIF value) 100；Pressure ambient
NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N], Alkaline phosphatase, 0.5 mM [U-100% 13C; U-100% 15N], Trigger Factor, 100 mM potassium chloride, 3 mM BME, 20 mM potassium phosphate, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
3BDF Crystal structure of metal-free E. coli alkaline phosphatase (T155V) Deposited 2007-11-14 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 22–471（450 aa）
Chain B 22–471（450 aa）
Mutation：T155V Mutation：T155V SO4 SULFATE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.1 M MES, 0.2 M LiSO4, 1 mM ZnCl2, 5 mM MgCl2, 25-30% PEG 3350, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.40 Å R-free 0.184
3BDG Crystal structure of wild-type/T155V mixed dimer of E. coli alkaline phosphatase Deposited 2007-11-14 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 22–471（450 aa）
Chain B 22–471（450 aa）
Mutation：T155V SO4 SULFATE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.1 M MES, 0.2 M LiSO4, 1 mM ZnCl2, 5 mM MgCl2, 25-30% PEG 3350, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.40 Å R-free 0.180
3BDH Crystal structure of zinc-deficient wild-type E. coli alkaline phosphatase Deposited 2007-11-14 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 22–471（450 aa）
Chain B 22–471（450 aa）
Not recorded MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.1 M MES, 0.2 M LiSO4, 1 mM ZnCl2, 5 mM MgCl2, 25-30% PEG 3350, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.85 Å R-free 0.189
3CMR E. coli alkaline phosphatase mutant R166S in complex with phosphate Deposited 2008-03-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：R166S Mutation：R166S ZN ZINC ION × 4 PO4 PHOSPHATE ION × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；298 K；22% PEG 3350, 0.2 M sodium citrate, 1 mM magnesium chloride, 5 mM sodium phosphate, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.05 Å R-free 0.213
3DPC Structure of E.coli Alkaline Phosphatase Mutant in Complex with a Phosphorylated Peptide Deposited 2008-07-07 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Mutation：S102L Mutation：S102L PO4 PHOSPHATE ION × 1 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.5；314 K；39%-43% saturation ammonium sulfate, 100mM Tris pH 9.5, VAPOR DIFFUSION, HANGING DROP, temperature 314K
Resolution 2.30 Å R-free 0.271
3DYC Structure of E322Y Alkaline Phosphatase in Complex with Inorganic Phosphate Deposited 2008-07-25 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 26–471（446 aa） Fragment：alkaline phosphatase
Chain B 26–471（446 aa） Fragment：alkaline phosphatase
Mutation：E322Y Mutation：E322Y ZN ZINC ION × 6 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；0.2 M ammonium fluoride, 20% PEG 3350, and 0.5 mM zinc chloride, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.30 Å R-free 0.243
3TG0 E. coli alkaline phosphatase with bound inorganic phosphate Deposited 2011-08-16 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa） Fragment：unp residues 23-471
Chain B 23–471（449 aa） Fragment：unp residues 23-471
Not recorded ZN ZINC ION × 4 MG MAGNESIUM ION × 2 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；20% PEG 4000, 0.2 M HEPES, 1 mM ZnCl2, 0.01 mM MgCl2, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.20 Å R-free 0.169
3TG0 E. coli alkaline phosphatase with bound inorganic phosphate Deposited 2011-08-16 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 23–471（449 aa） Fragment：unp residues 23-471
Chain D 23–471（449 aa） Fragment：unp residues 23-471
Not recorded ZN ZINC ION × 4 MG MAGNESIUM ION × 2 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；20% PEG 4000, 0.2 M HEPES, 1 mM ZnCl2, 0.01 mM MgCl2, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.20 Å R-free 0.169
4KM4 E. coli alkaline phosphatase mutant S102G/R166S in complex with inorganic phosphate Deposited 2013-05-08 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 26–470（445 aa）
Chain B 26–470（445 aa）
Mutation：S102G, R166S Mutation：S102G, R166S PO4 PHOSPHATE ION × 2 ZN ZINC ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；291 K；Equal parts 23.5 mg/mL enzyme in 10 mM NaMOPS and 50 mM NaCl and 0.2 M NH4F, 17-21% PEG 3350, and 500 uM ZnCl2, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 291K
Resolution 2.80 Å R-free 0.296
4YR1 Crystal Structure of E. Coli Alkaline Phosphatase D101A/D153A in complex with inorganic phosphate Deposited 2015-03-13 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 31–471（441 aa）
Chain B 31–471（441 aa）
Mutation：D101A D153A Mutation：D101A D153A ZN ZINC ION × 4 PO4 PHOSPHATE ION × 2 GOL GLYCEROL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；298 K；PEG 3350, Bis-Tris, ammonium sulfate, glycerol (cryo-protectant)
Resolution 2.24 Å R-free 0.259
5C66 E. Coli Alkaline Phosphatase in complex with tungstate Deposited 2015-06-22 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 23–471（449 aa）
Chain B 23–471（449 aa）
Not recorded ZN ZINC ION × 6 WO4 TUNGSTATE(VI)ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；291 K；sodium MOPS, sodium chloride, zinc chloride, magnesium chloride, PEG3350, ammonium fluoride, sodium tungstate
Resolution 2.03 Å R-free 0.240
5JTL The structure of chaperone SecB in complex with unstructured proPhoA Deposited 2016-05-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain E 1–471（471 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；301 K；Ionic strength (raw mmCIF value) 150；Pressure 1
NMR sample composition 300 uM [U-100% 13C; U-100% 15N] E.coli Chaperone SecB, 300 uM [U-100% 13C; U-100% 15N] E. Coli Alkaline Phosphatase (PhoA), 150 mM potassium chloride, 50 mM sodium phosphate, 50 mM potassium phosphate, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
5JTM The structure of chaperone SecB in complex with unstructured PhoA binding site a Deposited 2016-05-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain E 1–25（25 aa） Fragment：residues 1-25
Chain F 1–25（25 aa） Fragment：residues 1-25
Chain G 1–25（25 aa） Fragment：residues 1-25
Chain H 1–25（25 aa） Fragment：residues 1-25
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；301 K；Ionic strength (raw mmCIF value) 150；Pressure 1
NMR sample composition 300 uM [U-100% 13C; U-100% 15N] SecB, 300 uM [U-100% 13C; U-100% 15N] PhoA binding site a, 150 uM potassium chloride, 50 uM sodium phosphate, 50 uM potassium phosphate, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
5JTN The structure of chaperone SecB in complex with unstructured proPhoA binding site c Deposited 2016-05-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain E 91–145（55 aa） Fragment：residues 91-145
Chain F 91–145（55 aa） Fragment：residues 91-145
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；301 K；Ionic strength (raw mmCIF value) 150；Pressure 1
NMR sample composition 300 uM [U-100% 13C; U-100% 15N] E.coli Chaperone SecB, 300 uM [U-100% 13C; U-100% 15N] E.coli Alkaline Phosphatase (PhoA) binding site c, 150 mM potassium chloride, 50 mM sodium phosphate, 50 mM potassium phosphate, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
5JTO The structure of chaperone SecB in complex with unstructured proPhoA binding site d Deposited 2016-05-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain E 271–310（40 aa） Fragment：residues 271-310
Chain F 271–310（40 aa） Fragment：residues 271-310
Chain G 271–310（40 aa） Fragment：residues 271-310
Chain H 271–310（40 aa） Fragment：residues 271-310
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；301 K；Ionic strength (raw mmCIF value) 150；Pressure 1
NMR sample composition 300 uM [U-100% 13C; U-100% 15N] E.coli chaperone SecB, 300 uM [U-100% 13C; U-100% 15N] E.coli Alkaline Phosphatase (PhoA) binding site d, 150 mM potassium chloride, 50 mM sodium phosphate, 50 mM potassium phosphate, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
5JTP The structure of chaperone SecB in complex with unstructured proPhoA binding site e Deposited 2016-05-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain E 450–471（22 aa） Fragment：residues 450-471
Chain F 450–471（22 aa） Fragment：residues 450-471
Chain G 450–471（22 aa） Fragment：residues 450-471
Chain H 450–471（22 aa） Fragment：residues 450-471
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；301 K；Ionic strength (raw mmCIF value) 150；Pressure 1
NMR sample composition 300 uM [U-100% 13C; U-100% 15N] E.coli Chaperone SecB, 300 uM [U-100% 13C; U-100% 15N] E. Coli Alkaline Phosphatase (PhoA) binding site e, 150 mM potassium chloride, 50 mM sodium phosphate, 50 mM potassium phosphate, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
5TPQ E. coli alkaline phosphatase D101A, D153A, R166S, E322A, K328A mutant Deposited 2016-10-20 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 30–471（442 aa） Fragment：UNP residues 30-471
Chain B 30–471（442 aa） Fragment：UNP residues 30-471
Mutation：D101A, D153A, R166S, E322A, K328A Mutation：D101A, D153A, R166S, E322A, K328A ZN ZINC ION × 7 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；5 mg/mL protein in 10 mM MOPS pH 7.0, 50 mM NaCl, 100 mM ZnCl2. Protein solution mixed with equal volume of precipitant solution: 23% PEG 3350, 0.2 M NH3F, 0.2 M HEPES pH=8.0
Resolution 2.45 Å R-free 0.219
6PPT Structural Basis for Client Recognition and Activity of Hsp40 Chaperones Deposited 2019-07-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 4–13（10 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 120；Pressure 1
NMR sample composition 1 mM [U-13C; U-15N] PhoA-CBD1, 20 mM potassium phosphate, 75 mM potassium chloride, 0.04 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
6PQ2 Structural Basis for Client Recognition and Activity of Hsp40 Chaperones Deposited 2019-07-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 11–20（10 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100；Pressure 1
NMR sample composition 1 mM [U-100% 13C; U-100% 15N] L11-K20_CBD1, 20 mM potassium phosphate, 75 mM potassium chloride, 0.04 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
6PQE Structural Basis for Client Recognition and Activity of Hsp40 Chaperones Deposited 2019-07-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 235–245（11 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100；Pressure 1
NMR sample composition 1 mM [U-13C; U-15N] PhoA_235-245_DnaJ_191-256, 20 mM potassium phosphate, 75 mM potassium chloride, 0.04 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
6PQM Structural Basis for Client Recognition and Activity of Hsp40 Chaperones Deposited 2019-07-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 415–430（16 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100；Pressure 1
NMR sample composition 1 mM [U-100% 13C; U-100% 15N] PhoA-Hsp40/DnaJ CBD2 fusion, 75 mM potassium chloride, 20 mM potassium phosphate, 0.04 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
6PRI Structural Basis for Client Recognition and Activity of Hsp40 Chaperones Deposited 2019-07-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 437–447（11 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100；Pressure 1
NMR sample composition 1 mM [U-100% 13C; U-100% 15N] F-CBD2, 75 mM potassium chloride, 20 mM potassium phosphate, 0.04 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
6PRJ Structural Basis for Client Recognition and Activity of Hsp40 Chaperones Deposited 2019-07-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 457–467（11 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100；Pressure 1
NMR sample composition 1 mM [U-100% 13C; U-100% 15N] G-CBD2, 75 mM potassium chloride, 20 mM potassium phosphate, 0.04 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
6PRQ Structural Basis for Client Recognition and Activity of Hsp40 Chaperones Deposited 2019-07-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 179–187（9 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100；Pressure 1
NMR sample composition 1 mM [ILVMAT-sel-1H-13C_methyls; U-15N; U-2H] C-CBD1-CBD2, 75 mM potassium chloride, 20 mM potassium phosphate, 0.04 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1 mM [U-100% 13C; U-100% 15N] C-CBD1-CBD2, 75 mM potassium chloride, 20 mM potassium phosphate, 0.04 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
7JMM Crystal structure of the substrate-binding domain of E. coli DnaK in complex with the peptide RAKNIILLSR Deposited 2020-08-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 63–72（10 aa）
Mutation：P63R, I71S, G72R SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；2.4 M (NH4)2SO4, 0.1 M K3PO4
Resolution 2.56 Å R-free 0.327
7JN8 Crystal structure of the substrate-binding domain of E. coli DnaK in complex with the peptide RGNTLVIVSR Deposited 2020-08-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 381–390（10 aa）
Mutation：E381R, T389S, A390R SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；2.8 M (NH4)2SO4, 0.1 M K3PO4
Resolution 3.09 Å R-free 0.319
7JN9 Crystal structure of the substrate-binding domain of E. coli DnaK in complex with the peptide QEHTGSQLRIAAYGP Deposited 2020-08-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 432–446（15 aa）
Not recorded SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；2.4 M (NH4)2SO4, 0.1 M K3PO4
Resolution 2.40 Å R-free 0.286
7JNE Crystal structure of the substrate-binding domain of E. coli DnaK in complex with the peptide RGSQLRIASR Deposited 2020-08-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 435–444（10 aa）
Mutation：T435R, A443S, Y444R SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；2.4 M (NH4)2SO4, 0.1 M K3PO4
Resolution 2.54 Å R-free 0.334
7N6J Crystal structure of the substrate-binding domain of E. coli DnaK in complex with the peptide RKQSTIALALLPLLFTPRR Deposited 2021-06-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–19（19 aa）
Mutation：M1R, V18R, T19R SO4 SULFATE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；2.4 M (NH4)2SO4, 0.1 M K3PO4 pH 7.0
Resolution 2.00 Å R-free 0.265
7N6K Crystal structure of the substrate-binding domain of E. coli DnaK in complex with the peptide RALALLPLSR Deposited 2021-06-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 6–15（10 aa）
Mutation：I6R, L14S, F15R SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；293 K；2.6 M (NH4)2SO4, 0.1 M K3PO4
Resolution 2.55 Å R-free 0.306
7N6L Crystal structure of the substrate-binding domain of E. coli DnaK in complex with the peptide EANQQKPLLGLFADG Deposited 2021-06-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 270–284（15 aa）
Not recorded GOL GLYCEROL × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；2.8 M (NH4)2SO4, 0.1 M K3PO4
Resolution 2.40 Å R-free 0.332
7N6M Crystal structure of the substrate-binding domain of E. coli DnaK in complex with the peptide RQKPLLGLSR Deposited 2021-06-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 273–282（10 aa）
Mutation：Q273R, F281S, A282R SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；2.6 M (NH4)2SO4, 0.1 M K3PO4
Resolution 1.82 Å R-free 0.287

66 other PDB entries and 67 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PPB_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–446； UniProt 26–471 Author chain B； PDBConstruct 1–446； UniProt 26–471

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 1ura

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ura
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ura
Deposition date deposition_date1996-02-03
Structure title titleALKALINE PHOSPHATASE (D51ZN)
Keywords keywordsHYDROLASE, PHOSPHORIC MONOESTER, PHOSPHO TRANSFERASE, ALCOHOL ACCEPTOR, ALKALINE PHOSPHATASE; ALKALINE PHOSPHATASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier28.33 Å
Radius of gyration Rg (electron density) rg_electron27.77 Å
Forward intensity I(0) i0153118000.00
Molecular weight molecular_weight94054.0 kDa
Excluded volume excluded_volume115860 ų
Envelope volume envelope_volume133490 ų
Hydration-shell volume shell_volume39361 ų
Envelope diameter envelope_diameter104.7 Å
Shell Rg shell_rg35.80 Å
Envelope Rg envelope_rg28.16 Å
Shape Rg shape_rg27.78 Å
Total Rg total_rg28.40 Å
Total atoms total_atoms6586
Residues n_residues892
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax99.6 Å
Rg (real space) rg_real28.38 Å
Rg uncertainty (real space) rg_real_error0.84 Å
I(0) (real space) i0_real1.5310e+08
I(0) uncertainty (real space) i0_real_error2.4960e+06
Rg (reciprocal space) rg_reciprocal28.36 Å
I(0) (reciprocal space) i0_reciprocal153100000.0000
Solution quality estimate total_estimate0.8453
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.8 Å
Skewness Skewness skewness0.506
Kurtosis Kurtosis kurtosis0.076
Angular range angular_range— – 0.2800 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha39400000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.675; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.990
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1uraa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.76 — Alkaline phosphatase-like
Superfamily Superfamily superfamilyc.76.1 — Alkaline phosphatase-like
Family Family familyc.76.1.1 — Alkaline phosphatase
Domain ID domain_idd1urab_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.76 — Alkaline phosphatase-like
Superfamily Superfamily superfamilyc.76.1 — Alkaline phosphatase-like
Family Family familyc.76.1.1 — Alkaline phosphatase

CATH v4.4 (2 domains)

Domain ID domain_id1uraA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology720 — Alkaline Phosphatase, subunit A
Homologous superfamily homologous superfamily10 — Alkaline Phosphatase, subunit A
Domain ID domain_id1uraB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology720 — Alkaline Phosphatase, subunit A
Homologous superfamily homologous superfamily10 — Alkaline Phosphatase, subunit A
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8. Citations (4)

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9. Files and Curves (10)