1f93

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

Method: X-RAY DIFFRACTION

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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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	HEPATOCYTE NUCLEAR FACTOR 1-ALPHA × 2 （P22361） water × 3	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 4	HEPATOCYTE NUCLEAR FACTOR 1-ALPHA × 2 （P22361） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	DIMERIZATION COFACTOR OF HEPATOCYTE NUCLEAR FACTOR 1-ALPHA × 2 （P61459） water × 3	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 4	DIMERIZATION COFACTOR OF HEPATOCYTE NUCLEAR FACTOR 1-ALPHA × 2 （P61459） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

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. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1f93__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1f93__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1f93__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	20.43 Å
Rg (electron density)	19.25 Å
Total Rg	20.15 Å
Atom count	2052
Residues	256
Excluded volume	36481 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1f93__assembly_1__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1f93__assembly_2__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. 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

Source Source

Source organism organism	Rattus norvegicus
Common name common_name	Norway rat
NCBI taxonomy ID ncbi_taxonomy_id	10116
Host organism 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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6. 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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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

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

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1f93__assembly_1__model_1

1f93__assembly_1__model_1 | I(q)

1f93__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (8 domains)

CATH v4.4 (4 domains)

7. Citations (3)

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

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

HEPATOCYTE NUCLEAR FACTOR 1-ALPHA

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1f93__assembly_1__model_1

1f93__assembly_1__model_1 | I(q)

1f93__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (8 domains)

CATH v4.4 (4 domains)

7. Citations (3)