SAXSdb — 2ipt

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

IgG2a Fab fragment Heavy Chain

OrganismNot specified

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain L； UniProt 1–219	Not recorded	IgG2a Fab fragment Light Chain Kappa × 1 （Q6PIP8） ACM ACETAMIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；pH 7.5；294 K；0.1 M Hepes, 25% PEG3350, pH 7.5, VAPOR DIFFUSION, temperature 294K	Resolution 2.00 Å R-free 0.223

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 2IPT	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1ZEA Structure of the anti-cholera toxin antibody Fab fragment TE33 in complex with a D-peptide Deposited 2005-04-18	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain L 1–216（216 aa）	Not recorded	CIT CITRIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；PEG 8000, citrat buffer, potassium chloride, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.78 Å R-free 0.248
2DTM Thermodynamic and structural analyses of hydrolytic mechanism by catalytic antibodies Deposited 2006-07-13	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 1–219（219 aa） Fragment：FAB FRAGMENT	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.7；293 K；50mM Tris-HCl(pH 8.7), 16%(w/v) PEG4000, 0.1mM EDTA, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.25 Å R-free 0.278
2IQA PFA2 FAB fragment, monoclinic apo form Deposited 2006-10-13	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 1–219（219 aa）	Not recorded	ACM ACETAMIDE × 1 GOL GLYCEROL × 4 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；0.1 M Bis-Tris, 28% PEG-MME 2000, pH 6.5, VAPOR DIFFUSION	Resolution 2.00 Å R-free 0.279
2IQA PFA2 FAB fragment, monoclinic apo form Deposited 2006-10-13	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–219（219 aa）	Not recorded	ACM ACETAMIDE × 1 GOL GLYCEROL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；0.1 M Bis-Tris, 28% PEG-MME 2000, pH 6.5, VAPOR DIFFUSION	Resolution 2.00 Å R-free 0.279
2R0W PFA2 FAB complexed with Abeta1-8 Deposited 2007-08-21	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 L 1–219（219 aa） Fragment：light chain	Non-standard monomer：Yes (specific site not provided by mmCIF)	NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.3；295 K；25% PEG-MME 5000, 0.1 M OAc, pH 5.3, VAPOR DIFFUSION, temperature 295K	Resolution 2.50 Å R-free 0.277
2R0Z PFA1 FAB complexed with GripI peptide fragment Deposited 2007-08-21	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 L 1–219（219 aa） Fragment：light chain	Non-standard monomer：Yes (specific site not provided by mmCIF)	GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；295 K；PEG, VAPOR DIFFUSION, temperature 295K	Resolution 2.10 Å R-free 0.261
3EYS PFA1 Fab fragment complexed with pyro-Glu3-A-Beta (3-8) Deposited 2008-10-21	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 L 1–219（219 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；298 K；25% w/v PEG2000-MME, pH 8.5, vapor diffusion, sitting drop, temperature 298K	Resolution 1.95 Å R-free 0.256
3EYU PFA1 Fab fragment complexed with Ror2(518-525) Deposited 2008-10-21	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 L 1–219（219 aa）	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, SITTING DROP；298 K；20% w/v PEG3350, 0.2 M LiCl, vapor diffusion, sitting drop, temperature 298K	Resolution 2.71 Å R-free 0.248
4P3D MT1-MMP:Fab complex (Form II) Deposited 2014-03-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 1–217（217 aa） Chain L 1–217（217 aa）	Not recorded	CL CHLORIDE ION × 2 GOL GLYCEROL × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 EDO 1,2-ETHANEDIOL × 3 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；25% PEG 3350, 0.2M MgCl.hexahydrate, 0.1M Hepes	Resolution 1.95 Å R-free 0.210
4TPR Structure of Tau5 antibody Fab fragment Deposited 2014-06-09	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: Dimeric	Chain L 1–218（218 aa）	Not recorded	PG4 TETRAETHYLENE GLYCOL × 2 CL CHLORIDE ION × 5 PGE TRIETHYLENE GLYCOL × 1 NA SODIUM ION × 1 PEG DI(HYDROXYETHYL)ETHER × 5 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 33O 3,6,9,12,15,18,21,24,27,30,33,36-dodecaoxaoctatriacontane-1,38-diol × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；295 K；0.2 M NaCl, 0.1 M Bis-Tris, 25 % w/v PEG 3350	Resolution 1.60 Å R-free 0.191
4TQE Structure of tau peptide in complex with Tau5 antibody Fab fragment Deposited 2014-06-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain L 1–218（218 aa）	Not recorded	SO4 SULFATE ION × 5 NA SODIUM ION × 4 PGE TRIETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.2M lithium sulphate, 30% PEG 4000, 0.1M Tris pH 8.5	Resolution 1.60 Å R-free 0.197
6PXR Anti-TAU BIIB092 FAB with TAU peptide Deposited 2019-07-26	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain L 103–219（117 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；100 mM Tris-HCl, pH 8.5, 20% w/v PEG2000 MME, 200 mM trimethylamine N-oxide, 100 mM non-detergent sulfobetaine 201	Resolution 1.56 Å R-free 0.268
7A6C Nanodisc reconstituted human ABCB1 in complex with MRK16 Fab and elacridar Deposited 2020-08-25	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–219（219 aa）	Not recorded	R0Z elacridar × 2 CLR CHOLESTEROL × 10	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å

12 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A2NHM3_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain L； PDBConstruct 1–219； UniProt 1–219

IgG2a Fab fragment Light Chain Kappa

OrganismNot specified

UniProt Q6PIP8

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain H； UniProt 123–234	Not recorded	IgG2a Fab fragment Heavy Chain × 1 （A2NHM3） ACM ACETAMIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；pH 7.5；294 K；0.1 M Hepes, 25% PEG3350, pH 7.5, VAPOR DIFFUSION, temperature 294K	Resolution 2.00 Å R-free 0.223

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 2IPT	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 7 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 10 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain H 21–234（214 aa） Chain J 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 12 GOL GLYCEROL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 11 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain J 21–234（214 aa） Chain K 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 12 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 12 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain H 21–234（214 aa） Chain I 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 15 GOL GLYCEROL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain I 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 8 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain J 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 5 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain K 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 7	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain H 21–234（214 aa） Chain I 21–234（214 aa） Chain J 21–234（214 aa） Chain K 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 27 GOL GLYCEROL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain H 21–234（214 aa） Chain I 21–234（214 aa） Chain J 21–234（214 aa） Chain K 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 27 GOL GLYCEROL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 7 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain H 21–234（214 aa） Chain I 21–234（214 aa） Chain J 21–234（214 aa） Chain K 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 27 GOL GLYCEROL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 8 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain H 21–234（214 aa） Chain I 21–234（214 aa） Chain J 21–234（214 aa） Chain K 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 27 GOL GLYCEROL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 9 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain I 21–234（214 aa） Chain K 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 15 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
3J42 Obstruction of Dengue Virus Maturation by Fab Fragments of the 2H2 Antibody Deposited 2013-06-13	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 Heteromer；Protein × 720 PDB declaration: 720-meric	Chain G 120–230（111 aa） Fragment：SEE REMARK 999 Chain I 120–230（111 aa） Fragment：SEE REMARK 999 Chain K 120–230（111 aa） Fragment：SEE REMARK 999	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions 100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
3J42 Obstruction of Dengue Virus Maturation by Fab Fragments of the 2H2 Antibody Deposited 2013-06-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Heteromer；Protein × 12 PDB declaration: dodecameric	Chain G 120–230（111 aa） Fragment：SEE REMARK 999 Chain I 120–230（111 aa） Fragment：SEE REMARK 999 Chain K 120–230（111 aa） Fragment：SEE REMARK 999	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions 100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
3J42 Obstruction of Dengue Virus Maturation by Fab Fragments of the 2H2 Antibody Deposited 2013-06-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Insufficient information Heteromer；Protein × 60 PDB declaration: 60-meric	Chain G 120–230（111 aa） Fragment：SEE REMARK 999 Chain I 120–230（111 aa） Fragment：SEE REMARK 999 Chain K 120–230（111 aa） Fragment：SEE REMARK 999	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions 100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
3J42 Obstruction of Dengue Virus Maturation by Fab Fragments of the 2H2 Antibody Deposited 2013-06-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Insufficient information Heteromer；Protein × 72 PDB declaration: 72-meric	Chain G 120–230（111 aa） Fragment：SEE REMARK 999 Chain I 120–230（111 aa） Fragment：SEE REMARK 999 Chain K 120–230（111 aa） Fragment：SEE REMARK 999	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions 100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
3J42 Obstruction of Dengue Virus Maturation by Fab Fragments of the 2H2 Antibody Deposited 2013-06-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Insufficient information Heteromer；Protein × 12 PDB declaration: dodecameric	Chain G 120–230（111 aa） Fragment：SEE REMARK 999 Chain I 120–230（111 aa） Fragment：SEE REMARK 999 Chain K 120–230（111 aa） Fragment：SEE REMARK 999	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions 100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
4KVC 2H2 Fab fragment of immature Dengue virus Deposited 2013-05-22	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 120–230（111 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；25% PEG 6000 0.1 M MES 0.2M NH4Cl, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.31 Å R-free 0.234

3 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q6PIP8_MOUSE
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain H； PDBConstruct 112–223； UniProt 123–234

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2ipt
Deposition date deposition_date	2006-10-12
Structure title title	PFA1 Fab Fragment
Keywords keywords	wwddd, cdr, abeta, IMMUNE SYSTEM; IMMUNE SYSTEM
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	26.17 Å
Radius of gyration Rg (electron density) rg_electron	25.02 Å
Forward intensity I(0) i0	38720100.00
Molecular weight molecular_weight	47793.0 kDa
Excluded volume excluded_volume	59636 Å³
Envelope volume envelope_volume	73800 Å³
Hydration-shell volume shell_volume	24885 Å³
Envelope diameter envelope_diameter	81.8 Å
Shell Rg shell_rg	32.00 Å
Envelope Rg envelope_rg	24.60 Å
Shape Rg shape_rg	25.00 Å
Total Rg total_rg	25.86 Å
Total atoms total_atoms	3366
Residues n_residues	426
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	87.5 Å
Rg (real space) rg_real	26.15 Å
Rg uncertainty (real space) rg_real_error	0.51 Å
I(0) (real space) i0_real	3.8720e+07
I(0) uncertainty (real space) i0_real_error	5.5080e+05
Rg (reciprocal space) rg_reciprocal	26.16 Å
I(0) (reciprocal space) i0_reciprocal	38720000.0000
Solution quality estimate total_estimate	0.8183
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	27.3 Å
Skewness Skewness skewness	0.254
Kurtosis Kurtosis kurtosis	-0.608
Angular range angular_range	— – 0.3050 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	6611000.0000
Real-space data points n_real_points	62
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.894; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.953; Smooth: 0.000

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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	IgG2a Fab fragment Heavy Chain
Molecular weight formula_weight	24146.8 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	L
Atom count atom_count	3671

DVLMTQTPLSLPVSLGDQASISCRSSQSIVHSNGNTYLEWYLQKPGQSPKLLIYKVSNRFSGVPDRFSGSGSGTDFTLKISRVEAEDLGVYYCFQGSHVPLTFGAGTKLEIKRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC

Entity 2 Entity 2 polymer

Description description	IgG2a Fab fragment Light Chain Kappa
Molecular weight formula_weight	23811.8 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

QVTLKESGPGILKPSQTLSLTCSFSGFSLSTSGMGVGWIRQPSGKGLEWLAHIWWDDDKSYNPSLKSQLTISKDAARNQVFLRITSVDTADTATYYCVRRAHTTVLGDWFAYWGQGTLVTVSAAKTTAPSVYPLAPVCGGTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSGLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPR

Entity 3 Entity 3 non-polymer

Description description	ACETAMIDE
Molecular weight formula_weight	59.1 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	273

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7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d2ipth_
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.1 — V set domains (antibody variable domain-like)

Domain ID domain_id	d2iptl1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.1 — V set domains (antibody variable domain-like)

Domain ID domain_id	d2iptl2
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.2 — C1 set domains (antibody constant domain-like)

CATH v4.4 (4 domains)

Domain ID domain_id	2iptH01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	2iptH02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	2iptL01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	2iptL02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

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8. Citations (1)

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Unit-cell length a length_a	41.985 Å
Unit-cell length b length_b	42.825 Å
Unit-cell length c length_c	58.381 Å
Unit-cell angle α angle_alpha	95.84 °
Unit-cell angle β angle_beta	94.77 °
Unit-cell angle γ angle_gamma	91.91 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	25.190 Å
R factor r_factor	0.1800
R_work r_work	0.1770
R_free r_free	0.2230

fit	/app/data/saxs_computation/ip/2ipt/2ipt.fit
pddf	/app/data/pr_computation/ip/2ipt/2ipt.pr.out
profile	/app/data/saxs_computation/ip/2ipt/2ipt.dat

PFA1 Fab Fragment

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

IgG2a Fab fragment Heavy Chain

State in the Current Structure

Other States of the Same Protein in the Database

IgG2a Fab fragment Light Chain Kappa

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

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

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)