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8fdg

Cryo-EM structure of coagulation factor V short

Method: ELECTRON MICROSCOPY Dmax: 129.3 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Coagulation factor V

Homo sapiens

UniProt P12259

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 29–783 Chain A； UniProt 1487–2224 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE；2 second blot 20 second wait time Resolution 3.20 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 8FDG Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1CZS CRYSTAL STRUCTURE OF THE C2 DOMAIN OF HUMAN COAGULATION FACTOR V: COMPLEX WITH PHENYLMERCURY Deposited 1999-09-07 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2065–2224（160 aa） Fragment：C2 DISCOIDIN-LIKE DOMAIN
Not recorded PHG PHENYLMERCURY × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10.2；AMMONIUM SULFATE, pH 10.20, VAPOR DIFFUSION, HANGING DROP
Resolution 1.90 Å R-free 0.258
1CZT CRYSTAL STRUCTURE OF THE C2 DOMAIN OF HUMAN COAGULATION FACTOR V Deposited 1999-09-07 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2065–2224（160 aa） Fragment：C2 DISCOIDIN-LIKE DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10.2；AMMONIUM SULFATE, pH 10.20, VAPOR DIFFUSION, HANGING DROP
Resolution 1.87 Å R-free 0.242
1CZV CRYSTAL STRUCTURE OF THE C2 DOMAIN OF HUMAN COAGULATION FACTOR V: DIMERIC CRYSTAL FORM Deposited 1999-09-07 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2065–2224（160 aa） Fragment：C2 DISCOIDIN-LIKE DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 10；pH 10.00
Resolution 2.40 Å R-free 0.257
1CZV CRYSTAL STRUCTURE OF THE C2 DOMAIN OF HUMAN COAGULATION FACTOR V: DIMERIC CRYSTAL FORM Deposited 1999-09-07 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 2065–2224（160 aa） Fragment：C2 DISCOIDIN-LIKE DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 10；pH 10.00
Resolution 2.40 Å R-free 0.257
3P6Z Structural basis of thrombin mediated factor V activation: essential role of the hirudin-like sequence Glu666-Glu672 for processing at the heavy chain-B domain junction Deposited 2010-10-11 Different construct Different mutation/modification 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 C 685–737（53 aa） Fragment：FACTOR V, A2-B DOMAIN LINKER
Not recorded NA SODIUM ION × 3 0G6 D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-prolinamide × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CL CHLORIDE ION × 3 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；100 mM MOPS/HEPES-Na, pH 7.5, 12.5% (w/v) PEG 1000, 12.5% (w/v) PEG 3350, 12.5% (v/v) 2-methylpentane-2,4-diol (MPD), 30 mM Ca2+, 30 mM Mg2+, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.70 Å R-free 0.239
3P6Z Structural basis of thrombin mediated factor V activation: essential role of the hirudin-like sequence Glu666-Glu672 for processing at the heavy chain-B domain junction Deposited 2010-10-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain I 685–737（53 aa） Fragment：FACTOR V, A2-B DOMAIN LINKER
Not recorded NA SODIUM ION × 6 0G6 D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-prolinamide × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；100 mM MOPS/HEPES-Na, pH 7.5, 12.5% (w/v) PEG 1000, 12.5% (w/v) PEG 3350, 12.5% (v/v) 2-methylpentane-2,4-diol (MPD), 30 mM Ca2+, 30 mM Mg2+, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.70 Å R-free 0.239
3P70 Structural basis of thrombin-mediated factor V activation: essential role of the hirudin-like sequence Glu666-Glu672 for processing at the heavy chain-B domain junction Deposited 2010-10-11 Different construct Different mutation/modification 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 M 685–737（53 aa） Fragment：FACTOR V, A2-B DOMAIN LINKER
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 BEN BENZAMIDINE × 1 NA SODIUM ION × 2 BGC beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；100 mM MOPS/HEPES-Na, pH 7.5, 12.5% (w/v) PEG 1000, 12.5% (w/v) PEG 3350, 12.5% (v/v) 2-methylpentane-2,4-diol (MPD), 20 mM D-glucose, 20 mM D-mannose, 20 mM D-galactose, 20 mM L-fucose, 20 mM D-xylose, 20 mM N-acetyl-D-glucosamine , VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.55 Å R-free 0.279
3P70 Structural basis of thrombin-mediated factor V activation: essential role of the hirudin-like sequence Glu666-Glu672 for processing at the heavy chain-B domain junction Deposited 2010-10-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain N 685–737（53 aa） Fragment：FACTOR V, A2-B DOMAIN LINKER
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 BEN BENZAMIDINE × 1 NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；100 mM MOPS/HEPES-Na, pH 7.5, 12.5% (w/v) PEG 1000, 12.5% (w/v) PEG 3350, 12.5% (v/v) 2-methylpentane-2,4-diol (MPD), 20 mM D-glucose, 20 mM D-mannose, 20 mM D-galactose, 20 mM L-fucose, 20 mM D-xylose, 20 mM N-acetyl-D-glucosamine , VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.55 Å R-free 0.279
3P70 Structural basis of thrombin-mediated factor V activation: essential role of the hirudin-like sequence Glu666-Glu672 for processing at the heavy chain-B domain junction Deposited 2010-10-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Other combination Heteromer；Protein × 3 PDB declaration: trimeric
Chain O 685–737（53 aa） Fragment：FACTOR V, A2-B DOMAIN LINKER
Not recorded BEN BENZAMIDINE × 1 NA SODIUM ION × 1 BGC beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；100 mM MOPS/HEPES-Na, pH 7.5, 12.5% (w/v) PEG 1000, 12.5% (w/v) PEG 3350, 12.5% (v/v) 2-methylpentane-2,4-diol (MPD), 20 mM D-glucose, 20 mM D-mannose, 20 mM D-galactose, 20 mM L-fucose, 20 mM D-xylose, 20 mM N-acetyl-D-glucosamine , VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.55 Å R-free 0.279
3P70 Structural basis of thrombin-mediated factor V activation: essential role of the hirudin-like sequence Glu666-Glu672 for processing at the heavy chain-B domain junction Deposited 2010-10-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Other combination Heteromer；Protein × 3 PDB declaration: trimeric
Chain P 685–737（53 aa） Fragment：FACTOR V, A2-B DOMAIN LINKER
Not recorded BEN BENZAMIDINE × 1 NA SODIUM ION × 2 BGC beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；100 mM MOPS/HEPES-Na, pH 7.5, 12.5% (w/v) PEG 1000, 12.5% (w/v) PEG 3350, 12.5% (v/v) 2-methylpentane-2,4-diol (MPD), 20 mM D-glucose, 20 mM D-mannose, 20 mM D-galactose, 20 mM L-fucose, 20 mM D-xylose, 20 mM N-acetyl-D-glucosamine , VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.55 Å R-free 0.279
3S9C Russell's viper venom serine proteinase, RVV-V in complex with the fragment (residues 1533-1546) of human factor V Deposited 2011-06-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1561–1574（14 aa） Fragment：UNP residues 1561-1574
Not recorded BGC beta-D-glucopyranose × 1 GLC alpha-D-glucopyranose × 1 ACT ACETATE ION × 4 ZN ZINC ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；20% PEG 3350, 0.2M zinc acetate, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 1.80 Å R-free 0.218
7KVE Cryo-EM structure of human Factor V at 3.3 Angstrom resolution Deposited 2020-11-27 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 29–2224（2196 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, 5 mM CaCl2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
7KVF Cryo-EM structure of human Factor V at 3.6 Angstrom resolution Deposited 2020-11-28 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 29–2224（2196 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, 5 mM CaCl2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
7KXY Cryo-EM structure of human Factor Va at 4.4 Angstrom resolution Deposited 2020-12-05 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 29–737（709 aa） Fragment：UNP residues 29-737
Chain B 1574–2224（651 aa） Fragment：UNP residues 1574-2224
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, 5 mM CaCl2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.40 Å
7TPP Cryo-em structure of human prothrombin:prothrombinase at 4.1 Angstrom resolution Deposited 2022-01-25 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain C 29–737（709 aa） Fragment：domains A1 and A2 (UNP residues 29-737)
Chain D 1574–2224（651 aa） Fragment：domains C1, C2, and A3 (UNP residues 1574-2224)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；20mM Hepes, 150mM NaCl, 5mM CaCl2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.10 Å
8TN9 Structural architecture of the acidic region of the B domain of coagulation factor V Deposited 2023-08-01 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 29–2224（2196 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, 5 mM CaCl2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.05 Å
9CTH Preliminary map of the Prothrombin-prothrombinase complex on nano discs Deposited 2024-07-25 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain A 29–737（709 aa） Fragment：Domains A1 and A2 (UNP residues 29-737)
Chain E 1574–2224（651 aa） Fragment：Domains C1, C2, and A3 (UNP residues 1574-2224)
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, and 5 mM CaCl2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 6.47 Å
9I2H A 3.3 angstrom cryo-EM structure of an engineered high-affinity human prothrombinase complex Deposited 2025-01-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: pentameric
Chain A 29–737（709 aa）
Chain B 1574–2224（651 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 2 NA SODIUM ION × 1 0GJ L-alpha-glutamyl-N-{(1S)-4-{[amino(iminio)methyl]amino}-1-[(1S)-2-chloro-1-hydroxyethyl]butyl}glycinamide × 1 CU COPPER (II) ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5；20mM HEPES, 150mM NaCl and 5mM CaCl2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.28 Å
9MOT Cryo-EM structure of factor Va bound to activated protein C Deposited 2024-12-27 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 A 29–737（709 aa） Fragment：Domains A1 and A2 (UNP residues 29-737)
Chain B 1574–2224（651 aa） Fragment：Domains C1, C2, and A3 (UNP residues 1574-2224)
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, 5 mM CaCl2
cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, 5 mM CaCl2, 40uM n-Dodecyl-B-D-Maltoside
cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, 5 mM CaCl2
cryo-EM vitrification conditions Cryogen ETHANE
cryo-EM vitrification conditions Cryogen ETHANE
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.15 Å
9MOV Cryo-EM structure of factor Va bound to activated protein C Deposited 2024-12-27 Different construct 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 29–737（709 aa） Fragment：Domains A1 and A2 (UNP residues 29-737)
Chain B 1574–2224（651 aa） Fragment：Domains C1, C2, and A3 (UNP residues 1574-2224)
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 CA CALCIUM ION × 7 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, 5 mM CaCl2
cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, 5 mM CaCl2, 40uM n-Dodecyl-B-D-Maltoside
cryo-EM buffer pH 7.4；20 mM HEPES, 150 mM NaCl, 5 mM CaCl2
cryo-EM vitrification conditions Cryogen ETHANE
cryo-EM vitrification conditions Cryogen ETHANE
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
9YQ8 Cryo-EM complex of meizothrombinDESF1, factor Xa, and factor Va Deposited 2025-10-15 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain A 1574–2224（651 aa） Fragment：Domains C1, C2, and A3 (UNP residues 1574-2224)
Chain B 29–702（674 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.84 Å

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

View Construct and Data Evidence
UniProt name FA5_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–755； UniProt 29–783 Author chain A； PDBConstruct 756–1493； UniProt 1487–2224

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 8fdg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8fdg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8fdg
Deposition date deposition_date2022-12-03
Structure title titleCryo-EM structure of coagulation factor V short
Keywords keywordsBLOOD CLOTTING; BLOOD CLOTTING
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier38.93 Å
Radius of gyration Rg (electron density) rg_electron38.44 Å
Forward intensity I(0) i0457875000.00
Molecular weight molecular_weight172500.0 kDa
Excluded volume excluded_volume215010 ų
Envelope volume envelope_volume299660 ų
Hydration-shell volume shell_volume64302 ų
Envelope diameter envelope_diameter133.0 Å
Shell Rg shell_rg44.93 Å
Envelope Rg envelope_rg38.16 Å
Shape Rg shape_rg38.44 Å
Total Rg total_rg38.81 Å
Total atoms total_atoms12163
Residues n_residues1505
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 dmax129.3 Å
Rg (real space) rg_real38.90 Å
Rg uncertainty (real space) rg_real_error0.70 Å
I(0) (real space) i0_real4.5790e+08
I(0) uncertainty (real space) i0_real_error6.2620e+06
Rg (reciprocal space) rg_reciprocal38.92 Å
I(0) (reciprocal space) i0_reciprocal457900000.0000
Solution quality estimate total_estimate0.8729
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.3 Å
Skewness Skewness skewness0.378
Kurtosis Kurtosis kurtosis-0.223
Angular range angular_range— – 0.2050 Å−1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha95790000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.832; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.846
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id8fdgA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id8fdgA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily260 — Galactose-binding domain-like
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8. Citations (1)

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9. Files and Curves (10)