1nl5

Engineered High-affinity Maltose-Binding Protein

Method: X-RAY DIFFRACTION D_max: 67.9 Å Quality: EXCELLENT

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Maltose-binding periplasmic protein

Escherichia coli

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Other combination Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 27–396	Mutation：M321A Q325A, deletion of residues 172,173,175,176	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.5；PEG 3350, Zinc Chloride, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 100K	Resolution 2.10 Å R-free 0.290

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 1NL5	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1A7L DOMINANT B-CELL EPITOPE FROM THE PRES2 REGION OF HEPATITIS B VIRUS IN THE FORM OF AN INSERTED PEPTIDE SEGMENT IN MALTODEXTRIN-BINDING PROTEIN Deposited 1998-03-16	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–389（363 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；PROTEIN CONCENTRATION 3.0MG/ML, BUFFER 0.1M TRIS-HCL PH 8.5 WITH 0.2 M MGCL2, 1 MM MALTOSE, 26% PEG 4000.	Resolution 2.90 Å R-free 0.286
1A7L DOMINANT B-CELL EPITOPE FROM THE PRES2 REGION OF HEPATITIS B VIRUS IN THE FORM OF AN INSERTED PEPTIDE SEGMENT IN MALTODEXTRIN-BINDING PROTEIN Deposited 1998-03-16	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain B 27–389（363 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；PROTEIN CONCENTRATION 3.0MG/ML, BUFFER 0.1M TRIS-HCL PH 8.5 WITH 0.2 M MGCL2, 1 MM MALTOSE, 26% PEG 4000.	Resolution 2.90 Å R-free 0.286
1A7L DOMINANT B-CELL EPITOPE FROM THE PRES2 REGION OF HEPATITIS B VIRUS IN THE FORM OF AN INSERTED PEPTIDE SEGMENT IN MALTODEXTRIN-BINDING PROTEIN Deposited 1998-03-16	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain C 27–389（363 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；PROTEIN CONCENTRATION 3.0MG/ML, BUFFER 0.1M TRIS-HCL PH 8.5 WITH 0.2 M MGCL2, 1 MM MALTOSE, 26% PEG 4000.	Resolution 2.90 Å R-free 0.286
1A7L DOMINANT B-CELL EPITOPE FROM THE PRES2 REGION OF HEPATITIS B VIRUS IN THE FORM OF AN INSERTED PEPTIDE SEGMENT IN MALTODEXTRIN-BINDING PROTEIN Deposited 1998-03-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 27–389（363 aa） Chain B 27–389（363 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；PROTEIN CONCENTRATION 3.0MG/ML, BUFFER 0.1M TRIS-HCL PH 8.5 WITH 0.2 M MGCL2, 1 MM MALTOSE, 26% PEG 4000.	Resolution 2.90 Å R-free 0.286
1ANF MALTODEXTRIN BINDING PROTEIN WITH BOUND MALTOSE Deposited 1997-06-25	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；PROTEIN WAS CRYSTALLIZED FROM 18% PEG 8000, 10 MM CITRATE, PH 6.2	Resolution 1.67 Å
1DMB REFINED 1.8 ANGSTROMS STRUCTURE REVEALS THE MECHANISM OF BINDING OF A CYCLIC SUGAR, BETA-CYCLODEXTRIN, TO THE MALTODEXTRIN BINDING PROTEIN Deposited 1993-06-10	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.80 Å
1EZ9 STRUCTURE OF MALTOTETRAITOL BOUND TO OPEN-FORM MALTODEXTRIN BINDING PROTEIN IN P1 CRYSTAL FORM Deposited 2000-05-10	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.6；298 K；PEG 3350, MES, sodium azide, maltotetraitol, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 1.90 Å R-free 0.235
1EZ9 STRUCTURE OF MALTOTETRAITOL BOUND TO OPEN-FORM MALTODEXTRIN BINDING PROTEIN IN P1 CRYSTAL FORM Deposited 2000-05-10	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain B 27–396（370 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.6；298 K；PEG 3350, MES, sodium azide, maltotetraitol, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 1.90 Å R-free 0.235
1EZO GLOBAL FOLD OF MALTODEXTRIN BINDING PROTEIN COMPLEXED WITH BETA-CYCLODEXTRIN Deposited 2000-05-11	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Mutation：I28T	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.2；310 K；Pressure ambient NMR sample composition 1.4 mM maltodextrin binding protein U-15N,13C,2H, with 1H amide and methyl on Val, Leu, and Ile(delta1) 2mM beta-cyclodextrin, 20 mM sodium phosphate pH 7.2, 3uM NaN3, 100uM EDTA. \| 90% H2O/10% D2O	Resolution not provided
1EZP GLOBAL FOLD OF MALTODEXTRIN BINDING PROTEIN COMPLEXED WITH BETA-CYCLODEXTRIN USING PEPTIDE ORIENTATIONS FROM DIPOLAR COUPLINGS Deposited 2000-05-11	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Mutation：I28T	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.2；310 K；Pressure ambient NMR measurement conditions pH 7.2；310 K；Pressure ambient NMR sample composition 1.4 mM maltodextrin binding protein U-15N,13C,2H, with 1H amide and methyl on Val, Leu, and Ile(delta1) 2mM beta-cyclodextrin, 20 mM sodium phosphate pH 7.2, 3uM NaN3, 100uM EDTA. \| 90% H2O/10% D2O NMR sample composition 1.4 mM maltodextrin binding protein U-15N,13C,2H, with 1H amide and methyl on Val, Leu, and Ile(delta1) 2mM beta-cyclodextrin, 20 mM sodium phosphate pH 7.2, 3uM NaN3, 100uM EDTA. ~19mg/ml pf1 bacteriophage \| 90% H2O/10% D2O	Resolution not provided
1FQA STRUCTURE OF MALTOTETRAITOL BOUND TO OPEN-FORM MALTODEXTRIN BINDING PROTEIN IN P2(1)CRYSTAL FORM Deposited 2000-09-04	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.6；273 K；PEG 3350, NaN3, MES, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 273.0K	Resolution 1.90 Å R-free 0.215
1FQB STRUCTURE OF MALTOTRIOTOL BOUND TO OPEN-FORM MALTODEXTRIN BINDING PROTEIN IN P2(1)CRYSTAL FORM Deposited 2000-09-04	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.6；273 K；PEG 3350, NaN3, MES, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 273K	Resolution 1.90 Å R-free 0.218
1FQC CRYSTAL STRUCTURE OF MALTOTRIOTOL BOUND TO CLOSED-FORM MALTODEXTRIN BINDING PROTEIN Deposited 2000-09-04	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；293 K；PEG 6000, Mes, NaN3, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.30 Å R-free 0.246
1FQD CRYSTAL STRUCTURE OF MALTOTETRAITOL BOUND TO CLOSED-FORM MALTODEXTRIN BINDING PROTEIN Deposited 2000-09-04	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；293 K；PEG 6000, Mes, NaN3, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.30 Å R-free 0.244
1IUD MALTODEXTRIN-BINDING PROTEIN INSERTION/DELETION MUTANT WITH AN INSERTED B-CELL EPITOPE FROM THE PRES2 REGION OF HEPATITIS B VIRUS Deposited 1996-05-29	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Mutation：INSERTED B-CELL EPITOPE FROM THE PRES2 REGION OF HEPATITIS B VIRUS	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.70 Å R-free 0.281
1JVX Maltodextrin-binding protein variant D207C/A301GS/P316C cross-linked in crystal Deposited 2001-08-31	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Mutation：D207C/A301GS/P316C	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；277 K；PEG 6000, sodium MES, maltose, sodium azide, beta-mercaptoethanol, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.50 Å R-free 0.304
1JVY Maltodextrin-binding protein variant D207C/A301GS/P316C with beta-mercaptoethanol mixed disulfides Deposited 2001-08-31	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Mutation：D207C/A301GS/P316C Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；277 K；PEG 6000, sodium MES, maltose, sodium azide, beta-mercaptoethanol, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.273
1JW4 Structure of ligand-free maltodextrin-binding protein Deposited 2001-09-02	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；298 K；PEG 20k, Mes, sodium azide, pH 6.2, VAPOR DIFFUSION, HANGING DROP	Resolution 2.00 Å R-free 0.260
1JW5 Structure of Maltose Bound to Open-form Maltodextrin-binding Protein in P1 Crystal Deposited 2001-09-02	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；PEG 20k, Mes, sodium azide, pH 6.2, VAPOR DIFFUSION, HANGING DROP	Resolution 2.00 Å R-free 0.253
1LAX CRYSTAL STRUCTURE OF MALE31, A DEFECTIVE FOLDING MUTANT OF MALTOSE-BINDING PROTEIN Deposited 2002-03-29	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa） Fragment：MALE31	Mutation：G32D I33P	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；290 K；PEG 4000, TRIS/HCl, ISOPROPANOL, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 1.85 Å R-free 0.202
1LAX CRYSTAL STRUCTURE OF MALE31, A DEFECTIVE FOLDING MUTANT OF MALTOSE-BINDING PROTEIN Deposited 2002-03-29	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain C 27–396（370 aa） Fragment：MALE31	Mutation：G32D I33P	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；290 K；PEG 4000, TRIS/HCl, ISOPROPANOL, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 1.85 Å R-free 0.202
1LLS CRYSTAL STRUCTURE OF UNLIGANDED MALTOSE BINDING PROTEIN WITH XENON Deposited 2002-04-30	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Not recorded	XE XENON × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.6；298 K；10 mM Sodium Citrate, 23% PEG 8000, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.80 Å R-free 0.226
1MDP REFINED STRUCTURES OF TWO INSERTION(SLASH)DELETION MUTANTS PROBE FUNCTION OF THE MALTODEXTRIN BINDING PROTEIN Deposited 1994-08-10	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain 1 27–396（370 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å
1MDP REFINED STRUCTURES OF TWO INSERTION(SLASH)DELETION MUTANTS PROBE FUNCTION OF THE MALTODEXTRIN BINDING PROTEIN Deposited 1994-08-10	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain 2 27–396（370 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å
1MDQ REFINED STRUCTURES OF TWO INSERTION(SLASH)DELETION MUTANTS PROBE FUNCTION OF THE MALTODEXTRIN BINDING PROTEIN Deposited 1994-08-10	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.90 Å
1MG1 HTLV-1 GP21 ECTODOMAIN/MALTOSE-BINDING PROTEIN CHIMERA Deposited 1999-03-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 31–387（357 aa） Fragment：GP21 ECTODOMAIN (GP62 RESIDUES 338-425)	Not recorded	CL CHLORIDE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.7；pH 4.7	Resolution 2.50 Å R-free 0.305
1MH3 maltose binding-a1 homeodomain protein chimera, crystal form I Deposited 2002-08-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–392（366 aa）	Mutation：E359A, K362A, D363A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；298 K；amonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.10 Å R-free 0.262
1MH4 maltose binding-a1 homeodomain protein chimera, crystal form II Deposited 2002-08-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–392（366 aa）	Mutation：E359A, K362A, D363A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；PEG 6000, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.30 Å R-free 0.293
1MPB MALTODEXTRIN-BINDING PROTEIN (MALTOSE-BINDING PROTEIN) MUTANT, WITH ARGININE REPLACING TRYPTOPHAN AT POSITION 230 (TRP-230-ARG) Deposited 1995-07-25	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Mutation：W230R	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å
1MPC MALTODEXTRIN-BINDING PROTEIN (MALTOSE-BINDING PROTEIN) MUTANT, WITH ARGININE REPLACING TRYPTOPHAN AT POSITION 230 (TRP-230-ARG) Deposited 1995-07-25	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Mutation：W230R	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.10 Å
1MPD MALTODEXTRIN-BINDING PROTEIN (MALTOSE-BINDING PROTEIN) MUTANT, WITH ARGININE REPLACING TRYPTOPHAN AT POSITION 230 (TRP-230-ARG), COMPLEXED WITH MALTOSE Deposited 1995-07-25	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Mutation：W230R	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å
1N3W Engineered High-Affinity Maltose-Binding Protein Deposited 2002-10-29	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Mutation：Deletion of residues 172,173,175,176	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；290 K；PEG 4000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 2.60 Å R-free 0.295
1N3X Ligand-free High-Affinity Maltose-Binding Protein Deposited 2002-10-29	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Mutation：Deletion of residues 172,173,175,176.	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；290 K；PEG 4000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 2.50 Å R-free 0.241
1NMU MBP-L30 Deposited 2003-01-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 27–392（366 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；Sodium Citrate, Tris, Sodium Chloride, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.31 Å R-free 0.254
1NMU MBP-L30 Deposited 2003-01-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 27–392（366 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；Sodium Citrate, Tris, Sodium Chloride, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.31 Å R-free 0.254
1OMP CRYSTALLOGRAPHIC EVIDENCE OF A LARGE LIGAND-INDUCED HINGE-TWIST MOTION BETWEEN THE TWO DOMAINS OF THE MALTODEXTRIN-BINDING PROTEIN INVOLVED IN ACTIVE TRANSPORT AND CHEMOTAXIS Deposited 1992-09-14	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.80 Å
1PEB LIGAND-FREE HIGH-AFFINITY MALTOSE-BINDING PROTEIN Deposited 2003-05-21	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Mutation：M321A, Q325A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；312 K；PEG 3500, cacodylic acid, zinc acetate, sodium chloride, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 312K	Resolution 2.60 Å R-free 0.242
1R6Z The Crystal Structure of the Argonaute2 PAZ domain (as a MBP fusion) Deposited 2003-10-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 27–392（366 aa） Fragment：MBP (residues 28-392) fused with Argonaute2 PAZ domain (residues 591-726) Chain P 27–392（366 aa） Fragment：MBP (residues 28-392) fused with Argonaute2 PAZ domain (residues 591-726) Chain Z 27–392（366 aa） Fragment：MBP (residues 28-392) fused with Argonaute2 PAZ domain (residues 591-726)	Not recorded	NI NICKEL (II) ION × 9	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；290 K；PEG2KMME, NiCl2, TrisHCl, NaF, meso-erythritol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 2.80 Å R-free 0.281
1R6Z The Crystal Structure of the Argonaute2 PAZ domain (as a MBP fusion) Deposited 2003-10-17	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain P 27–392（366 aa） Fragment：MBP (residues 28-392) fused with Argonaute2 PAZ domain (residues 591-726)	Not recorded	NI NICKEL (II) ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；290 K；PEG2KMME, NiCl2, TrisHCl, NaF, meso-erythritol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 2.80 Å R-free 0.281
1R6Z The Crystal Structure of the Argonaute2 PAZ domain (as a MBP fusion) Deposited 2003-10-17	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–392（366 aa） Fragment：MBP (residues 28-392) fused with Argonaute2 PAZ domain (residues 591-726)	Not recorded	NI NICKEL (II) ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；290 K；PEG2KMME, NiCl2, TrisHCl, NaF, meso-erythritol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 2.80 Å R-free 0.281
1R6Z The Crystal Structure of the Argonaute2 PAZ domain (as a MBP fusion) Deposited 2003-10-17	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain Z 27–392（366 aa） Fragment：MBP (residues 28-392) fused with Argonaute2 PAZ domain (residues 591-726)	Not recorded	NI NICKEL (II) ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；290 K；PEG2KMME, NiCl2, TrisHCl, NaF, meso-erythritol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 2.80 Å R-free 0.281
1SVX Crystal structure of a designed selected Ankyrin Repeat protein in complex with the Maltose Binding Protein Deposited 2004-03-30	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 29–392（364 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；30% PEG 6000, 0.1M Tris, 0.1M NaCl, pH 8-9, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.24 Å R-free 0.249
1T0K Joint X-ray and NMR Refinement of Yeast L30e-mRNA complex Deposited 2004-04-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 2 PDB declaration: tetrameric	Chain A 27–392（366 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；295 K；Lithium Sulfate, Sodium Cacodylate, Magnesium Chloride, Jeffamine, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 3.24 Å R-free 0.320
1Y4C Designed Helical Protein fusion MBP Deposited 2004-11-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–392（366 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.90 Å R-free 0.225
1YTV Maltose-binding protein fusion to a C-terminal fragment of the V1a vasopressin receptor Deposited 2005-02-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 27–392（366 aa） Fragment：c-terminal residues 27-392 Chain B 27–392（366 aa） Fragment：c-terminal residues 27-392	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；295 K；0.2M Ammonium sulfate, 25%(v/v)PEG 400 and 25%(v/v) glycerol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.80 Å R-free 0.225
1ZIU Crystal Structure of nickel-bound engineered Maltose Binding Protein Deposited 2005-04-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa） Fragment：residues 27-396	Mutation：A63H, R66H, E111M, Y155E, W340E	NI NICKEL (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；PEG 2000 MME, sodium acetate, nickel chloride, Tris-HCl, sodium chloride, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.00 Å R-free 0.243
1ZJL Crystal structure of zinc-bound engineered maltose binding protein Deposited 2005-04-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa） Fragment：residues 27-396	Mutation：A63H, R66H, E111M, Y155E, W340E	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；PEG 2000 MME, sodium acetate, zinc acetate, HEPES, sodium chloride, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.00 Å R-free 0.232
1ZKB Zinc-free Engineered maltose binding protein Deposited 2005-05-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa） Fragment：RESIDUES 27-396	Mutation：A66H, R63H, E111M, Y155E, W340E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；PEG 2000 MME, sodium acetate, Tris-HcL, sodium chloride, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.20 Å R-free 0.285
1ZMG Crystal structure of copper-bound engineered maltose binding protein Deposited 2005-05-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa） Fragment：RESIDUES 27-396	Mutation：A63H, R66H, E111M, Y155E, W340E	CU COPPER (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；PEG 2000 MME, copper sulphate, sodium acetate, Tris-HCl, sodium chloride, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.50 Å R-free 0.268
3MBP MALTODEXTRIN-BINDING PROTEIN WITH BOUND MALTOTRIOSE Deposited 1997-06-25	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；PROTEIN WAS CRYSTALLIZED FROM 18% PEG 8000, 10 MM CITRATE, PH 6.2	Resolution 1.70 Å
4MBP MALTODEXTRIN BINDING PROTEIN WITH BOUND MALTETROSE Deposited 1997-08-17	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–396（370 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；PROTEIN WAS CRYSTALLIZED FROM 18% PEG 8000, 10 MM CITRATE, PH 6.2	Resolution 1.70 Å

41 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MALE_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–366； UniProt 27–396

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1nl5
Deposition date deposition_date	2003-01-06
Structure title title	Engineered High-affinity Maltose-Binding Protein
Keywords keywords	MBP, MALTOSE-BINDING PROTEIN, HIGH-AFFINITY MUTANT, Maltodextrin-Binding Protein, SUGAR BINDING PROTEIN; SUGAR BINDING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	21.67 Å
Radius of gyration Rg (electron density) rg_electron	20.58 Å
Forward intensity I(0) i0	25952400.00
Molecular weight molecular_weight	40439.0 kDa
Excluded volume excluded_volume	51178 Å³
Envelope volume envelope_volume	57518 Å³
Hydration-shell volume shell_volume	23083 Å³
Envelope diameter envelope_diameter	69.3 Å
Shell Rg shell_rg	27.36 Å
Envelope Rg envelope_rg	20.80 Å
Shape Rg shape_rg	20.52 Å
Total Rg total_rg	21.65 Å
Total atoms total_atoms	2856
Residues n_residues	366
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	67.9 Å
Rg (real space) rg_real	21.57 Å
Rg uncertainty (real space) rg_real_error	0.34 Å
I(0) (real space) i0_real	2.5950e+07
I(0) uncertainty (real space) i0_real_error	3.3510e+05
Rg (reciprocal space) rg_reciprocal	21.59 Å
I(0) (reciprocal space) i0_reciprocal	25950000.0000
Solution quality estimate total_estimate	0.9026
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	26.4 Å
Skewness Skewness skewness	0.237
Kurtosis Kurtosis kurtosis	-0.420
Angular range angular_range	— – 0.3650 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	5710000.0000
Real-space data points n_real_points	68
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.911; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.998

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Maltose-binding periplasmic protein
Molecular weight formula_weight	40100.4 kDa
Mutation mutation	M321A Q325A, deletion of residues 172,173,175,176
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	3167

KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYGDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATAENAAKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTRITK

来源 Source

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 branched

Description description	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose
Molecular weight formula_weight	342.3 kDa
Source method src_method	man
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	311

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1nl5a_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamily	c.94.1 — Periplasmic binding protein-like II
Family Family family	c.94.1.1 — Phosphate binding protein-like

CATH v4.4 (2 domains)

Domain ID domain_id	1nl5A01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

Domain ID domain_id	1nl5A02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

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8. Citations (1)

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Unit-cell length a length_a	121.590 Å
Unit-cell length b length_b	121.590 Å
Unit-cell length c length_c	62.440 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 43 21 2
Space-group number int_tables_number	96
Crystal system crystal_system	—

Resolution resolution	2.100 Å
Low-resolution limit resolution_low	60.800 Å
R factor r_factor	0.2520
R_work r_work	0.2520
R_free r_free	0.2900

fit	/app/data/saxs_computation/nl/1nl5/1nl5.fit
pddf	/app/data/pr_computation/nl/1nl5/1nl5.pr.out
profile	/app/data/saxs_computation/nl/1nl5/1nl5.dat