SAXSdb — 1f93

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

DIMERIZATION COFACTOR OF HEPATOCYTE NUCLEAR FACTOR 1-ALPHA

Rattus norvegicus

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 1–104 Chain B； UniProt 1–104	Non-standard monomer：Yes (specific site not provided by mmCIF)	HEPATOCYTE NUCLEAR FACTOR 1-ALPHA × 2 （P22361）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；PEG 8000, potassium succinate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.60 Å R-free 0.299
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain C； UniProt 1–104 Chain D； UniProt 1–104	Non-standard monomer：Yes (specific site not provided by mmCIF)	HEPATOCYTE NUCLEAR FACTOR 1-ALPHA × 2 （P22361）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；PEG 8000, potassium succinate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.60 Å R-free 0.299

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 1F93	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1DCH CRYSTAL STRUCTURE OF DCOH, A BIFUNCTIONAL, PROTEIN-BINDING TRANSCRIPTION COACTIVATOR Deposited 1995-01-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–103（103 aa） Chain B 1–103（103 aa） Chain C 1–103（103 aa） Chain D 1–103（103 aa）	Not recorded	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.2；pH 7.2 COMPND ROOM TEMP., 1.7M AMSO4, .1M HEPES, PH 7.2.	Resolution 3.00 Å
1DCH CRYSTAL STRUCTURE OF DCOH, A BIFUNCTIONAL, PROTEIN-BINDING TRANSCRIPTION COACTIVATOR Deposited 1995-01-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain E 1–103（103 aa） Chain F 1–103（103 aa） Chain G 1–103（103 aa） Chain H 1–103（103 aa）	Not recorded	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.2；pH 7.2 COMPND ROOM TEMP., 1.7M AMSO4, .1M HEPES, PH 7.2.	Resolution 3.00 Å
1DCO DCOH, A BIFUNCTIONAL PROTEIN-BINDING TRANSCRIPTIONAL COACTIVATOR Deposited 1996-05-16	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–103（103 aa） Chain B 1–103（103 aa） Chain C 1–103（103 aa） Chain D 1–103（103 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；ROOM TEMPERATURE, 1.7M AMSO4, 0.1M HEPES, PH 7.4	Resolution 2.30 Å
1DCO DCOH, A BIFUNCTIONAL PROTEIN-BINDING TRANSCRIPTIONAL COACTIVATOR Deposited 1996-05-16	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain E 1–103（103 aa） Chain F 1–103（103 aa） Chain G 1–103（103 aa） Chain H 1–103（103 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；ROOM TEMPERATURE, 1.7M AMSO4, 0.1M HEPES, PH 7.4	Resolution 2.30 Å
1DCP DCOH, A BIFUNCTIONAL PROTEIN-BINDING TRANSCRIPTIONAL COACTIVATOR, COMPLEXED WITH BIOPTERIN Deposited 1996-05-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–103（103 aa） Chain B 1–103（103 aa） Chain C 1–103（103 aa） Chain D 1–103（103 aa）	Not recorded	HBI 7,8-DIHYDROBIOPTERIN × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；ROOM TEMPERATURE, 1.7M AMSO4, 0.1M HEPES, PH 7.4	Resolution 2.30 Å
1DCP DCOH, A BIFUNCTIONAL PROTEIN-BINDING TRANSCRIPTIONAL COACTIVATOR, COMPLEXED WITH BIOPTERIN Deposited 1996-05-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain E 1–103（103 aa） Chain F 1–103（103 aa） Chain G 1–103（103 aa） Chain H 1–103（103 aa）	Not recorded	HBI 7,8-DIHYDROBIOPTERIN × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；ROOM TEMPERATURE, 1.7M AMSO4, 0.1M HEPES, PH 7.4	Resolution 2.30 Å
3HXA Crystal Structure of DCoH1Thr51Ser Deposited 2009-06-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–104（104 aa） Chain B 1–104（104 aa） Chain C 1–104（104 aa） Chain D 1–104（104 aa）	Mutation：T51S Mutation：T51S Mutation：T51S Mutation：T51S	SO4 SULFATE ION × 4 GOL GLYCEROL × 3	X-RAY DIFFRACTION X-ray crystallization conditions Hanging drop；pH 7.5；291 K；HEPES, Ammonium Sulfate, PEG 200, Glycerol, pH 7.5, Hanging drop, temperature 291K	Resolution 1.80 Å R-free 0.226
3HXA Crystal Structure of DCoH1Thr51Ser Deposited 2009-06-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain E 1–104（104 aa） Chain F 1–104（104 aa） Chain G 1–104（104 aa） Chain H 1–104（104 aa）	Mutation：T51S Mutation：T51S Mutation：T51S Mutation：T51S	SO4 SULFATE ION × 4 GOL GLYCEROL × 5	X-RAY DIFFRACTION X-ray crystallization conditions Hanging drop；pH 7.5；291 K；HEPES, Ammonium Sulfate, PEG 200, Glycerol, pH 7.5, Hanging drop, temperature 291K	Resolution 1.80 Å R-free 0.226

4 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PHS_RAT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–104； UniProt 1–104 Author chain B； PDBConstruct 1–104； UniProt 1–104 Author chain C； PDBConstruct 1–104； UniProt 1–104 Author chain D； PDBConstruct 1–104； UniProt 1–104

HEPATOCYTE NUCLEAR FACTOR 1-ALPHA

OrganismNot specified

UniProt P22361

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain E； UniProt 1–32 Chain F； UniProt 1–32	Fragment：DIMERIZATION DOMAIN (RESIDUES 1-32)	DIMERIZATION COFACTOR OF HEPATOCYTE NUCLEAR FACTOR 1-ALPHA × 2 （P61459）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；PEG 8000, potassium succinate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.60 Å R-free 0.299
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain G； UniProt 1–32 Chain H； UniProt 1–32	Fragment：DIMERIZATION DOMAIN (RESIDUES 1-32)	DIMERIZATION COFACTOR OF HEPATOCYTE NUCLEAR FACTOR 1-ALPHA × 2 （P61459）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；PEG 8000, potassium succinate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.60 Å R-free 0.299

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 1F93	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1G2Y HNF-1ALPHA DIMERIZATION DOMAIN, WITH SELENOMETHIONINE SUBSTITUED AT LEU 12 Deposited 2000-10-23	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUES 1-32 Chain C 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUES 1-32	Mutation：L12(MSE) Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：L12(MSE) 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 8.5；277 K；PEG 4000, Tris-HCl, lithium sulphate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 1.00 Å R-free 0.198
1G2Y HNF-1ALPHA DIMERIZATION DOMAIN, WITH SELENOMETHIONINE SUBSTITUED AT LEU 12 Deposited 2000-10-23	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUES 1-32 Chain D 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUES 1-32	Mutation：L12(MSE) Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：L12(MSE) 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 8.5；277 K；PEG 4000, Tris-HCl, lithium sulphate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 1.00 Å R-free 0.198
1G2Y HNF-1ALPHA DIMERIZATION DOMAIN, WITH SELENOMETHIONINE SUBSTITUED AT LEU 12 Deposited 2000-10-23	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUES 1-32 Chain B 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUES 1-32 Chain C 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUES 1-32 Chain D 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUES 1-32	Mutation：L12(MSE) Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：L12(MSE) Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：L12(MSE) Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：L12(MSE) 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 8.5；277 K；PEG 4000, Tris-HCl, lithium sulphate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 1.00 Å R-free 0.198
1G2Y HNF-1ALPHA DIMERIZATION DOMAIN, WITH SELENOMETHIONINE SUBSTITUED AT LEU 12 Deposited 2000-10-23	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUES 1-32 Chain B 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUES 1-32 Chain C 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUES 1-32 Chain D 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUES 1-32	Mutation：L12(MSE) Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：L12(MSE) Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：L12(MSE) Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：L12(MSE) 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 8.5；277 K；PEG 4000, Tris-HCl, lithium sulphate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 1.00 Å R-free 0.198
1G2Z DIMERIZATION DOMAIN OF HNF-1ALPHA WITH A LEU 13 SELENOMETHIONINE SUBSTITUTION Deposited 2000-10-23	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUES 1-32 Chain B 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUES 1-32	Mutation：L13(MSE) Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：L13(MSE) 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 8.5；277 K；PEG 4000, Tris-HCl, lithium sulphate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 1.15 Å R-free 0.243
1G39 WILD-TYPE HNF-1ALPHA DIMERIZATION DOMAIN Deposited 2000-10-23	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUE 1-32 Chain C 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUE 1-32	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；PEG 4000, Tris-HCl, lithium sulphate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 1.22 Å R-free 0.278
1G39 WILD-TYPE HNF-1ALPHA DIMERIZATION DOMAIN Deposited 2000-10-23	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUE 1-32 Chain D 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUE 1-32	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；PEG 4000, Tris-HCl, lithium sulphate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 1.22 Å R-free 0.278
1G39 WILD-TYPE HNF-1ALPHA DIMERIZATION DOMAIN Deposited 2000-10-23	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUE 1-32 Chain B 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUE 1-32 Chain C 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUE 1-32 Chain D 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUE 1-32	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；PEG 4000, Tris-HCl, lithium sulphate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 1.22 Å R-free 0.278
1G39 WILD-TYPE HNF-1ALPHA DIMERIZATION DOMAIN Deposited 2000-10-23	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUE 1-32 Chain B 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUE 1-32 Chain C 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUE 1-32 Chain D 1–32（32 aa） Fragment：DIMERIZATION DOMAIN, RESIDUE 1-32	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；PEG 4000, Tris-HCl, lithium sulphate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 1.22 Å R-free 0.278
1JB6 Crystal Structure of Dimerization Domain (1-33) of HNF-1alpha Deposited 2001-06-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–33（33 aa） Fragment：Dimerization domain (residues 1-32)	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 7.5；277 K；MPD, Tris-HCl, DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.70 Å R-free 0.245
1JB6 Crystal Structure of Dimerization Domain (1-33) of HNF-1alpha Deposited 2001-06-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 1–33（33 aa） Fragment：Dimerization domain (residues 1-32)	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 7.5；277 K；MPD, Tris-HCl, DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.70 Å R-free 0.245
1JB6 Crystal Structure of Dimerization Domain (1-33) of HNF-1alpha Deposited 2001-06-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–33（33 aa） Fragment：Dimerization domain (residues 1-32) Chain B 1–33（33 aa） Fragment：Dimerization domain (residues 1-32)	Non-standard monomer：Yes (specific site not provided by mmCIF) 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 7.5；277 K；MPD, Tris-HCl, DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.70 Å R-free 0.245
1JB6 Crystal Structure of Dimerization Domain (1-33) of HNF-1alpha Deposited 2001-06-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–33（33 aa） Fragment：Dimerization domain (residues 1-32) Chain B 1–33（33 aa） Fragment：Dimerization domain (residues 1-32)	Non-standard monomer：Yes (specific site not provided by mmCIF) 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 7.5；277 K；MPD, Tris-HCl, DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.70 Å R-free 0.245
1LFB THE X-RAY STRUCTURE OF AN ATYPICAL HOMEODOMAIN PRESENT IN THE RAT LIVER TRANSCRIPTION FACTOR LFB1(SLASH)HNF1 AND IMPLICATIONS FOR DNA BINDING Deposited 1993-06-28	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 195–286（92 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å R-free 0.364

5 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	HNF1A_MOUSE
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain E； PDBConstruct 1–32； UniProt 1–32 Author chain F； PDBConstruct 1–32； UniProt 1–32 Author chain G； PDBConstruct 1–32； UniProt 1–32 Author chain H； PDBConstruct 1–32； UniProt 1–32

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	1f93
Deposition date deposition_date	2000-07-06
Structure title title	CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THE DIMERIZATION DOMAIN OF HNF-1 ALPHA AND THE COACTIVATOR DCOH
Keywords keywords	four-helix bundle, transcriptional activator-coactivator complex, dimerization domain, TRANSCRIPTION; TRANSCRIPTION
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	30.47 Å
Radius of gyration Rg (electron density) rg_electron	29.63 Å
Forward intensity I(0) i0	54609900.00
Molecular weight molecular_weight	57637.0 kDa
Excluded volume excluded_volume	71790 Å³
Envelope volume envelope_volume	92620 Å³
Hydration-shell volume shell_volume	27170 Å³
Envelope diameter envelope_diameter	105.1 Å
Shell Rg shell_rg	35.30 Å
Envelope Rg envelope_rg	29.48 Å
Shape Rg shape_rg	29.67 Å
Total Rg total_rg	30.05 Å
Total atoms total_atoms	4044
Residues n_residues	504
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	101.2 Å
Rg (real space) rg_real	30.63 Å
Rg uncertainty (real space) rg_real_error	0.75 Å
I(0) (real space) i0_real	5.4610e+07
I(0) uncertainty (real space) i0_real_error	9.3010e+05
Rg (reciprocal space) rg_reciprocal	30.56 Å
I(0) (reciprocal space) i0_reciprocal	54610000.0000
Solution quality estimate total_estimate	0.8709
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	29.2 Å
Skewness Skewness skewness	0.417
Kurtosis Kurtosis kurtosis	-0.458
Angular range angular_range	— – 0.2600 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	10530000.0000
Real-space data points n_real_points	53
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.884; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.833; Smooth: 0.833

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	DIMERIZATION COFACTOR OF HEPATOCYTE NUCLEAR FACTOR 1-ALPHA
Molecular weight formula_weight	12158.3 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	4106

MAGKAHRLSAEERDQLLPNLRAVGWNELEGRDAIFKQFHFKDFNRAFGFMTRVALQAEKLDHHPEWFNVYNKVHITLSTHECAGLSERDINLASFIEQVAVSMT

来源 Source

来源生物 organism	Rattus norvegicus
通用名 common_name	Norway rat
NCBI Class编号 ncbi_taxonomy_id	10116
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	HEPATOCYTE NUCLEAR FACTOR 1-ALPHA
Molecular weight formula_weight	3387.0 kDa
Source method src_method	syn
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,F,G,H

MVSKLSQLQTELLAALLESGLSKEALIQALGE

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	62

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7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d1f93a_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.74 — DCoH-like
Superfamily Superfamily superfamily	d.74.1 — PCD-like
Family Family family	d.74.1.1 — PCD-like

Domain ID domain_id	d1f93b_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.74 — DCoH-like
Superfamily Superfamily superfamily	d.74.1 — PCD-like
Family Family family	d.74.1.1 — PCD-like

Domain ID domain_id	d1f93c_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.74 — DCoH-like
Superfamily Superfamily superfamily	d.74.1 — PCD-like
Family Family family	d.74.1.1 — PCD-like

Domain ID domain_id	d1f93d_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.74 — DCoH-like
Superfamily Superfamily superfamily	d.74.1 — PCD-like
Family Family family	d.74.1.1 — PCD-like

Domain ID domain_id	d1f93e_
Class class	a — All alpha proteins
Fold Fold fold	a.34 — Dimerisation interlock
Superfamily Superfamily superfamily	a.34.2 — Dimerization cofactor of HNF-1 alpha
Family Family family	a.34.2.1 — Dimerization cofactor of HNF-1 alpha

Domain ID domain_id	d1f93f_
Class class	a — All alpha proteins
Fold Fold fold	a.34 — Dimerisation interlock
Superfamily Superfamily superfamily	a.34.2 — Dimerization cofactor of HNF-1 alpha
Family Family family	a.34.2.1 — Dimerization cofactor of HNF-1 alpha

Domain ID domain_id	d1f93g_
Class class	a — All alpha proteins
Fold Fold fold	a.34 — Dimerisation interlock
Superfamily Superfamily superfamily	a.34.2 — Dimerization cofactor of HNF-1 alpha
Family Family family	a.34.2.1 — Dimerization cofactor of HNF-1 alpha

Domain ID domain_id	d1f93h_
Class class	a — All alpha proteins
Fold Fold fold	a.34 — Dimerisation interlock
Superfamily Superfamily superfamily	a.34.2 — Dimerization cofactor of HNF-1 alpha
Family Family family	a.34.2.1 — Dimerization cofactor of HNF-1 alpha

CATH v4.4 (4 domains)

Domain ID domain_id	1f93A00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily	20 — Transcriptional coactivator/pterin dehydratase

Domain ID domain_id	1f93B00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily	20 — Transcriptional coactivator/pterin dehydratase

Domain ID domain_id	1f93C00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily	20 — Transcriptional coactivator/pterin dehydratase

Domain ID domain_id	1f93D00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily	20 — Transcriptional coactivator/pterin dehydratase

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8. Citations (3)

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Unit-cell length a length_a	49.480 Å
Unit-cell length b length_b	82.750 Å
Unit-cell length c length_c	70.640 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	97.83 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.600 Å
Low-resolution limit resolution_low	20.100 Å
R factor r_factor	0.2570
R_work r_work	0.2570
R_free r_free	0.2990

fit	/app/data/saxs_computation/f9/1f93/1f93.fit
pddf	/app/data/pr_computation/f9/1f93/1f93.pr.out
profile	/app/data/saxs_computation/f9/1f93/1f93.dat

CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THE DIMERIZATION DOMAIN OF HNF-1 ALPHA AND THE COACTIVATOR DCOH

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

DIMERIZATION COFACTOR OF HEPATOCYTE NUCLEAR FACTOR 1-ALPHA

State in the Current Structure

Other States of the Same Protein in the Database

HEPATOCYTE NUCLEAR FACTOR 1-ALPHA

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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (8 domains)

CATH v4.4 (4 domains)

8. Citations (3)

9. Files and Curves (10)

Files (7)

Curves (3)