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1dcp

DCOH, A BIFUNCTIONAL PROTEIN-BINDING TRANSCRIPTIONAL COACTIVATOR, COMPLEXED WITH BIOPTERIN

Method: X-RAY DIFFRACTION Dmax: 114.5 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

DCOH

Rattus norvegicus

UniProt P61459

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain A； UniProt 1–103 Chain B； UniProt 1–103 Chain C； UniProt 1–103 Chain D； UniProt 1–103 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
2 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain E； UniProt 1–103 Chain F； UniProt 1–103 Chain G； UniProt 1–103 Chain H； UniProt 1–103 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

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 1DCP 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 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 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 ligand/ion 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 ligand/ion 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
1F93 CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THE DIMERIZATION DOMAIN OF HNF-1 ALPHA AND THE COACTIVATOR DCOH Deposited 2000-07-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–104（104 aa）
Chain B 1–104（104 aa）
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 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
1F93 CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THE DIMERIZATION DOMAIN OF HNF-1 ALPHA AND THE COACTIVATOR DCOH Deposited 2000-07-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1–104（104 aa）
Chain D 1–104（104 aa）
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 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
3HXA Crystal Structure of DCoH1Thr51Ser Deposited 2009-06-20 Different construct Different mutation/modification 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 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 2–104； UniProt 1–103 Author chain B； PDBConstruct 2–104； UniProt 1–103 Author chain C； PDBConstruct 2–104； UniProt 1–103 Author chain D； PDBConstruct 2–104； UniProt 1–103 Author chain E； PDBConstruct 2–104； UniProt 1–103 Author chain F； PDBConstruct 2–104； UniProt 1–103 Author chain G； PDBConstruct 2–104； UniProt 1–103 Author chain H； PDBConstruct 2–104； UniProt 1–103

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

SAXS scattering curve SAXS Profile

SAXS profile for 1dcp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1dcp
Deposition date deposition_date1996-05-16
Structure title titleDCOH, A BIFUNCTIONAL PROTEIN-BINDING TRANSCRIPTIONAL COACTIVATOR, COMPLEXED WITH BIOPTERIN
Keywords keywords;TRANSCRIPTIONAL STIMULATOR, DIMERIZATION COFACTOR, DEHYDRATASE, 4A-CARBINOLAMINE DEHYDRATASE, TRANSREGULATOR OF HOMEODOMAIN PROTEINS ;; TRANSCRIPTIONAL STIMULATOR
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier35.49 Å
Radius of gyration Rg (electron density) rg_electron34.86 Å
Forward intensity I(0) i0141616000.00
Molecular weight molecular_weight93619.0 kDa
Excluded volume excluded_volume116140 ų
Envelope volume envelope_volume149110 ų
Hydration-shell volume shell_volume36494 ų
Envelope diameter envelope_diameter117.0 Å
Shell Rg shell_rg40.25 Å
Envelope Rg envelope_rg34.64 Å
Shape Rg shape_rg34.83 Å
Total Rg total_rg35.31 Å
Total atoms total_atoms6623
Residues n_residues792
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax114.5 Å
Rg (real space) rg_real35.57 Å
Rg uncertainty (real space) rg_real_error0.88 Å
I(0) (real space) i0_real1.4160e+08
I(0) uncertainty (real space) i0_real_error2.2950e+06
Rg (reciprocal space) rg_reciprocal35.53 Å
I(0) (reciprocal space) i0_reciprocal141600000.0000
Solution quality estimate total_estimate0.8948
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary35.6 Å
Skewness Skewness skewness0.292
Kurtosis Kurtosis kurtosis-0.714
Angular range angular_range— – 0.2250 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11390000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.916; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.942; Smooth: 0.939
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd1dcpa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.74 — DCoH-like
Superfamily Superfamily superfamilyd.74.1 — PCD-like
Family Family familyd.74.1.1 — PCD-like
Domain ID domain_idd1dcpb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.74 — DCoH-like
Superfamily Superfamily superfamilyd.74.1 — PCD-like
Family Family familyd.74.1.1 — PCD-like
Domain ID domain_idd1dcpc_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.74 — DCoH-like
Superfamily Superfamily superfamilyd.74.1 — PCD-like
Family Family familyd.74.1.1 — PCD-like
Domain ID domain_idd1dcpd_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.74 — DCoH-like
Superfamily Superfamily superfamilyd.74.1 — PCD-like
Family Family familyd.74.1.1 — PCD-like
Domain ID domain_idd1dcpe_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.74 — DCoH-like
Superfamily Superfamily superfamilyd.74.1 — PCD-like
Family Family familyd.74.1.1 — PCD-like
Domain ID domain_idd1dcpf_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.74 — DCoH-like
Superfamily Superfamily superfamilyd.74.1 — PCD-like
Family Family familyd.74.1.1 — PCD-like
Domain ID domain_idd1dcpg_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.74 — DCoH-like
Superfamily Superfamily superfamilyd.74.1 — PCD-like
Family Family familyd.74.1.1 — PCD-like
Domain ID domain_idd1dcph_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.74 — DCoH-like
Superfamily Superfamily superfamilyd.74.1 — PCD-like
Family Family familyd.74.1.1 — PCD-like

CATH v4.4 (8 domains)

Domain ID domain_id1dcpA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily20 — Transcriptional coactivator/pterin dehydratase
Domain ID domain_id1dcpB00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily20 — Transcriptional coactivator/pterin dehydratase
Domain ID domain_id1dcpC00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily20 — Transcriptional coactivator/pterin dehydratase
Domain ID domain_id1dcpD00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily20 — Transcriptional coactivator/pterin dehydratase
Domain ID domain_id1dcpE00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily20 — Transcriptional coactivator/pterin dehydratase
Domain ID domain_id1dcpF00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily20 — Transcriptional coactivator/pterin dehydratase
Domain ID domain_id1dcpG00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily20 — Transcriptional coactivator/pterin dehydratase
Domain ID domain_id1dcpH00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily20 — Transcriptional coactivator/pterin dehydratase
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8. Citations (2)

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9. Files and Curves (10)