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2q0a

Structure and rearrangements in the carboxy-terminal region of SpIH channels

Method: X-RAY DIFFRACTION Dmax: 78.7 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2

Mus musculus

UniProt O88703

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 443–640 Fragment：C-TERMINAL DOMAIN (residues 443-640) Mutation：I636D PCG CYCLIC GUANOSINE MONOPHOSPHATE × 4 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；10 % w/v PEG 8000, 0.5 M NaCl, 15 % Glycerol, 0.1 M MES, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.25 Å R-free 0.261
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain B； UniProt 443–640 Fragment：C-TERMINAL DOMAIN (residues 443-640) Mutation：I636D PCG CYCLIC GUANOSINE MONOPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；10 % w/v PEG 8000, 0.5 M NaCl, 15 % Glycerol, 0.1 M MES, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.25 Å R-free 0.261
3 Protein homooligomer Homooligomer Protein × 8 PDB declaration: octameric（8） Consistent with protein copy count Chain A； UniProt 443–640 Chain B； UniProt 443–640 Fragment：C-TERMINAL DOMAIN (residues 443-640) Mutation：I636D PCG CYCLIC GUANOSINE MONOPHOSPHATE × 8 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；10 % w/v PEG 8000, 0.5 M NaCl, 15 % Glycerol, 0.1 M MES, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.25 Å R-free 0.261
4 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain B； UniProt 443–640 Fragment：C-TERMINAL DOMAIN (residues 443-640) Mutation：I636D PCG CYCLIC GUANOSINE MONOPHOSPHATE × 4 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；10 % w/v PEG 8000, 0.5 M NaCl, 15 % Glycerol, 0.1 M MES, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.25 Å R-free 0.261

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 2Q0A Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1Q3E HCN2J 443-645 in the presence of cGMP Deposited 2003-07-29 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 443–645（203 aa） Fragment：Residues 443-645 (Reference sequence numbering)
Not recorded PCG CYCLIC GUANOSINE MONOPHOSPHATE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；277 K；PEG 400, sodium citrate, sodium chloride, DTT, HEPES, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.90 Å R-free 0.239
1Q3E HCN2J 443-645 in the presence of cGMP Deposited 2003-07-29 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain B 443–645（203 aa） Fragment：Residues 443-645 (Reference sequence numbering)
Not recorded PCG CYCLIC GUANOSINE MONOPHOSPHATE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；277 K；PEG 400, sodium citrate, sodium chloride, DTT, HEPES, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.90 Å R-free 0.239
1Q3E HCN2J 443-645 in the presence of cGMP Deposited 2003-07-29 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric
Chain A 443–645（203 aa） Fragment：Residues 443-645 (Reference sequence numbering)
Chain B 443–645（203 aa） Fragment：Residues 443-645 (Reference sequence numbering)
Not recorded PCG CYCLIC GUANOSINE MONOPHOSPHATE × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；277 K；PEG 400, sodium citrate, sodium chloride, DTT, HEPES, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.90 Å R-free 0.239
1Q43 HCN2I 443-640 in the presence of cAMP, selenomethionine derivative Deposited 2003-08-01 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 443–645（203 aa） Fragment：residues 443-645
Non-standard monomer：Yes (specific site not provided by mmCIF) CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；277 K；PEG 400, sodium citrate, sodium chloride, DTT, HEPES, cAMP, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.00 Å R-free 0.242
1Q43 HCN2I 443-640 in the presence of cAMP, selenomethionine derivative Deposited 2003-08-01 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 443–645（203 aa） Fragment：residues 443-645
Non-standard monomer：Yes (specific site not provided by mmCIF) CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；277 K；PEG 400, sodium citrate, sodium chloride, DTT, HEPES, cAMP, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.00 Å R-free 0.242
1Q43 HCN2I 443-640 in the presence of cAMP, selenomethionine derivative Deposited 2003-08-01 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric
Chain A 443–645（203 aa） Fragment：residues 443-645
Chain B 443–645（203 aa） Fragment：residues 443-645
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；277 K；PEG 400, sodium citrate, sodium chloride, DTT, HEPES, cAMP, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.00 Å R-free 0.242
1Q43 HCN2I 443-640 in the presence of cAMP, selenomethionine derivative Deposited 2003-08-01 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain B 443–645（203 aa） Fragment：residues 443-645
Non-standard monomer：Yes (specific site not provided by mmCIF) CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；277 K；PEG 400, sodium citrate, sodium chloride, DTT, HEPES, cAMP, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.00 Å R-free 0.242
1Q5O HCN2J 443-645 in the presence of cAMP, selenomethionine derivative Deposited 2003-08-08 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 443–645（203 aa） Fragment：Residues 443-645
Non-standard monomer：Yes (specific site not provided by mmCIF) CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；277 K；PEG 400, sodium citrate, sodium chloride, DTT, HEPES, cAMP, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.30 Å R-free 0.261
3BPZ HCN2-I 443-460 E502K in the presence of cAMP Deposited 2007-12-19 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 443–640（198 aa） Fragment：ligand biding domain (residues 443-640)
Chain B 443–640（198 aa） Fragment：ligand biding domain (residues 443-640)
Chain C 443–640（198 aa） Fragment：ligand biding domain (residues 443-640)
Chain D 443–640（198 aa） Fragment：ligand biding domain (residues 443-640)
Mutation：E502K Mutation：E502K Mutation：E502K Mutation：E502K CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 4.6；279 K；PEG 400, SODIUM CITRATE, SODIUM CHLORIDE, DTT, HEPES, 5 mM CAMP, pH 4.6, VAPOR DIFFUSION, temperature 279K
Resolution 1.65 Å R-free 0.216
3ETQ X-ray structure of cysteine-free fragment of mHCN2 C-terminal region from amino acids 443-630 including C508N, C584S, and C601S mutations Deposited 2008-10-08 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric
Chain A 443–640（198 aa） Fragment：C-terminal fragment
Chain B 443–640（198 aa） Fragment：C-terminal fragment
Mutation：C508N, C584S, C601S Mutation：C508N, C584S, C601S CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；16% w/v PEG 6000, 500 mM NaCl, 10% glycerol, 100 mM citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.90 Å R-free 0.216
3FFQ HCN2I 443-640 apo-state Deposited 2008-12-04 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 443–640（198 aa）
Not recorded BR BROMIDE ION × 20 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；Two uL protein (5-7 mg/mL) mixed with one uL reservoir solution composed of 0.4 M NaCl, 0.1 NaBr, 0.1 M MES, pH 6.0, 20% glycerol (v/v), and 20% PEG 8000 (w/v). Crystals grew within eight weeks and harvested an additional eight weeks after initial growth, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.40 Å R-free 0.283
3FFQ HCN2I 443-640 apo-state Deposited 2008-12-04 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 B 443–640（198 aa）
Not recorded BR BROMIDE ION × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；Two uL protein (5-7 mg/mL) mixed with one uL reservoir solution composed of 0.4 M NaCl, 0.1 NaBr, 0.1 M MES, pH 6.0, 20% glycerol (v/v), and 20% PEG 8000 (w/v). Crystals grew within eight weeks and harvested an additional eight weeks after initial growth, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.40 Å R-free 0.283
4EQF Trip8b-1a#206-567 interacting with the carboxy-terminal seven residues of HCN2 Deposited 2012-04-18 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 857–863（7 aa） Fragment：UNP residues 857-863
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；298 K；91mM MES, 91mM triSodium citrate, 3.63M NaCL, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 3.00 Å R-free 0.281
5JON Crystal structure of the unliganded form of HCN2 CNBD Deposited 2016-05-02 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 494–640（147 aa）
Not recorded NO3 NITRATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；34-36% dimethyl PEG 500, 240 mM potassium nitrate, 20 mM magnesium chloride, 100 mM BIS-TRIS, pH 6.0
Resolution 2.04 Å R-free 0.221
5JON Crystal structure of the unliganded form of HCN2 CNBD Deposited 2016-05-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain B 494–640（147 aa）
Not recorded NO3 NITRATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；34-36% dimethyl PEG 500, 240 mM potassium nitrate, 20 mM magnesium chloride, 100 mM BIS-TRIS, pH 6.0
Resolution 2.04 Å R-free 0.221
5KHG HCN2 CNBD in complex with cytidine-3', 5'-cyclic monophosphate (cCMP) Deposited 2016-06-14 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 443–643（201 aa） Fragment：UNP residues 443-643
Non-standard monomer：Yes (specific site not provided by mmCIF) CC7 4-amino-1-[(2S,4aR,6R,7R,7aS)-2,7-dihydroxy-2-oxidotetrahydro-4H-furo[3,2-d][1,3,2]dioxaphosphinin-6-yl]pyrimidin-2(1H)-one × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；277 K；200 mM NaCl, 0.1 mM sodium citrate pH 5.0, 16% PEG 400
Resolution 2.24 Å R-free 0.264
5KHH HCN2 CNBD in complex with inosine-3', 5'-cyclic monophosphate (cIMP) Deposited 2016-06-14 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 443–643（201 aa） Fragment：UNP residues 443-643
Non-standard monomer：Yes (specific site not provided by mmCIF) 6SW Inosine-3',5'-cyclic monophosphate × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；200 mM NaCl, 0.1 mM sodium citrate pH 5.5, 14.5% PEG 400
Resolution 1.77 Å R-free 0.263
5KHI HCN2 CNBD in complex with purine riboside-3', 5'-cyclic monophosphate (cPuMP) Deposited 2016-06-14 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 443–643（201 aa） Fragment：UNP residues 443-643
Non-standard monomer：Yes (specific site not provided by mmCIF) 6SX Purine riboside-3',5'-cyclic monophosphate × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；200 mM NaCl, 0.1 mM sodium citrate pH 5.5, 18% PEG 400
Resolution 2.10 Å R-free 0.249
5KHJ HCN2 CNBD in complex with uridine-3', 5'-cyclic monophosphate (cUMP) Deposited 2016-06-14 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 443–643（201 aa） Fragment：UNP residues 443-643
Chain B 443–643（201 aa） Fragment：UNP residues 443-643
Not recorded 6SY Uridine-3',5'-cyclic monophosphate × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；277 K；200 mM NaCl, 0.1 mM sodium citrate pH 4.6, 13% PEG 400
Resolution 2.01 Å R-free 0.252
5KHK HCN2 CNBD in complex with 2-aminopurine riboside-3', 5'-cyclic monophosphate (2-NH2-cPuMP) Deposited 2016-06-14 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 443–643（201 aa） Fragment：UNP residues 443-643
Non-standard monomer：Yes (specific site not provided by mmCIF) 6SZ 2-Aminopurine riboside-3',5'-cyclic monophosphate × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；277 K；200 mM NaCl, 0.1 mM sodium citrate pH 4.6, 12% PEG 400
Resolution 2.07 Å R-free 0.261
9R1T Structure of the human chimera HCN112 hyperpolarization-activated cyclic nucleotide-gated ion channel in complex with cAMP. Deposited 2025-04-28 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 Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 444–647（204 aa）
Chain B 444–647（204 aa）
Chain C 444–647（204 aa）
Chain D 444–647（204 aa）
Not recorded CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.34 Å

14 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HCN2_MOUSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 3–200； UniProt 443–640 Author chain B； PDBConstruct 3–200； UniProt 443–640

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 2q0a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2q0a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2q0a
Deposition date deposition_date2007-05-21
Structure title titleStructure and rearrangements in the carboxy-terminal region of SpIH channels
Keywords keywordsHCN2, ion channel, cyclic nucleotide binding domain, C-linker, cGMP, TRANSPORT PROTEIN; TRANSPORT PROTEIN
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_guinier25.68 Å
Radius of gyration Rg (electron density) rg_electron24.72 Å
Forward intensity I(0) i037877200.00
Molecular weight molecular_weight46301.0 kDa
Excluded volume excluded_volume57547 ų
Envelope volume envelope_volume73954 ų
Hydration-shell volume shell_volume25164 ų
Envelope diameter envelope_diameter79.7 Å
Shell Rg shell_rg31.56 Å
Envelope Rg envelope_rg24.56 Å
Shape Rg shape_rg24.68 Å
Total Rg total_rg25.67 Å
Total atoms total_atoms3252
Residues n_residues388
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 dmax78.7 Å
Rg (real space) rg_real25.61 Å
Rg uncertainty (real space) rg_real_error0.42 Å
I(0) (real space) i0_real3.7880e+07
I(0) uncertainty (real space) i0_real_error4.9610e+05
Rg (reciprocal space) rg_reciprocal25.63 Å
I(0) (reciprocal space) i0_reciprocal37880000.0000
Solution quality estimate total_estimate0.9129
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary31.8 Å
Skewness Skewness skewness0.193
Kurtosis Kurtosis kurtosis-0.548
Angular range angular_range— – 0.3100 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4407000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.974; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.941
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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) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2q0aa_
Class classb — All beta proteins
Fold Fold foldb.82 — Double-stranded beta-helix
Superfamily Superfamily superfamilyb.82.3 — cAMP-binding domain-like
Family Family familyb.82.3.2 — cAMP-binding domain
Domain ID domain_idd2q0ab_
Class classb — All beta proteins
Fold Fold foldb.82 — Double-stranded beta-helix
Superfamily Superfamily superfamilyb.82.3 — cAMP-binding domain-like
Family Family familyb.82.3.2 — cAMP-binding domain

CATH v4.4 (4 domains)

Domain ID domain_id2q0aA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily630 — Helix hairpin bin
Domain ID domain_id2q0aA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily10 — Jelly Rolls
Domain ID domain_id2q0aB01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily630 — Helix hairpin bin
Domain ID domain_id2q0aB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily10 — Jelly Rolls
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8. Citations (1)

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9. Files and Curves (10)