1j34

Crystal Structure of Mg(II)-and Ca(II)-bound Gla Domain of Factor IX Complexed with Binding Protein

Method: X-RAY DIFFRACTION Dmax: 79.7 Å Quality: GOOD

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

coagulation factor IX-binding protein A chain

OrganismNot specified

UniProt P23806

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–129 Not recorded coagulation factor IX-binding protein B chain × 1 (P23807) Coagulation factor IX × 1 (P00741) CA CALCIUM ION × 7 MG MAGNESIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 8;293 K;PEG 6000, Tris-HCl, calcium chloride, magnesium chloride, pH 8, MICROBATCH, temperature 293K Resolution 1.55 Å R-free 0.212

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.

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

View Construct and Data Evidence
UniProt name IXA_TRIFL
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–129; UniProt 1–129

coagulation factor IX-binding protein B chain

OrganismNot specified

UniProt P23807

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 24–146 Not recorded coagulation factor IX-binding protein A chain × 1 (P23806) Coagulation factor IX × 1 (P00741) CA CALCIUM ION × 7 MG MAGNESIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 8;293 K;PEG 6000, Tris-HCl, calcium chloride, magnesium chloride, pH 8, MICROBATCH, temperature 293K Resolution 1.55 Å R-free 0.212

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.

5 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IXB_TRIFL
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–123; UniProt 24–146

Coagulation factor IX

OrganismNot specified

UniProt P00741

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–46 Fragment:GLA DOMAIN Non-standard monomer:Yes (specific site not provided by mmCIF) coagulation factor IX-binding protein A chain × 1 (P23806) coagulation factor IX-binding protein B chain × 1 (P23807) CA CALCIUM ION × 7 MG MAGNESIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 8;293 K;PEG 6000, Tris-HCl, calcium chloride, magnesium chloride, pH 8, MICROBATCH, temperature 293K Resolution 1.55 Å R-free 0.212

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FA9_BOVIN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–46; UniProt 1–46

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 1j34

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1j34
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1j34
Deposition date deposition_date2003-01-20
Structure title titleCrystal Structure of Mg(II)-and Ca(II)-bound Gla Domain of Factor IX Complexed with Binding Protein
Keywords keywordsMAGNESIUM ION, CALCIUM ION, GLA DOMAIN, Protein binding-Blood clotting COMPLEX; Protein binding/Blood clotting
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier21.55
Radius of gyration Rg (electron density) rg_electron20.78
Forward intensity I(0) i023638100.00
Molecular weight molecular_weight35616.0 kDa
Excluded volume excluded_volume43637 ų
Envelope volume envelope_volume49104 ų
Hydration-shell volume shell_volume20416 ų
Envelope diameter envelope_diameter81.4
Shell Rg shell_rg26.80
Envelope Rg envelope_rg21.07
Shape Rg shape_rg20.78
Total Rg total_rg21.51
Total atoms total_atoms2490
Residues n_residues286
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax79.7
Rg (real space) rg_real21.63
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real2.3640e+07
I(0) uncertainty (real space) i0_real_error3.2640e+05
Rg (reciprocal space) rg_reciprocal21.62
I(0) (reciprocal space) i0_reciprocal23640000.0000
Solution quality estimate total_estimate0.8198
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.4
Skewness Skewness skewness0.499
Kurtosis Kurtosis kurtosis-0.051
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6196000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.620; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.799; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1j34a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.169 — C-type lectin-like
Superfamily Superfamily superfamilyd.169.1 — C-type lectin-like
Family Family familyd.169.1.1 — C-type lectin domain
Domain ID domain_idd1j34b_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.169 — C-type lectin-like
Superfamily Superfamily superfamilyd.169.1 — C-type lectin-like
Family Family familyd.169.1.1 — C-type lectin domain
Domain ID domain_idd1j34c_
Class classg — Small proteins
Fold Fold foldg.32 — GLA-domain
Superfamily Superfamily superfamilyg.32.1 — GLA-domain
Family Family familyg.32.1.1 — GLA-domain

CATH v4.4 (2 domains)

Domain ID domain_id1j34A00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology100 — Mannose-Binding Protein A; Chain A
Homologous superfamily homologous superfamily10 — Mannose-Binding Protein A, subunit A
Domain ID domain_id1j34B00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology100 — Mannose-Binding Protein A; Chain A
Homologous superfamily homologous superfamily10 — Mannose-Binding Protein A, subunit A

8. Citations (3)

9. Files and Curves (10)