1x2w

Crystal Structure of Apo-Habu IX-bp at pH 4.6

Method: X-RAY DIFFRACTION Dmax: 80.8 Å Quality: GOOD

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

Coagulation factor IX/X-binding protein A chain

OrganismNot specified

UniProt Q7LZ71

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–129 Not recorded Coagulation factor IX/factor X-binding protein B chain × 1 (P23807) CL CHLORIDE ION × 1 RB RUBIDIUM ION × 2 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;293 K;AMMONIUM SULPHATE, RUBIDIUM ACETATE, PEGMME 2000, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.29 Å R-free 0.280
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–129 Not recorded Coagulation factor IX/factor X-binding protein B chain × 2 (P23807) CL CHLORIDE ION × 2 RB RUBIDIUM ION × 4 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;293 K;AMMONIUM SULPHATE, RUBIDIUM ACETATE, PEGMME 2000, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.29 Å R-free 0.280

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 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q7LZ71_TRIFL
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–129; UniProt 1–129

Coagulation factor IX/factor X-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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 24–146 Not recorded Coagulation factor IX/X-binding protein A chain × 1 (Q7LZ71) CL CHLORIDE ION × 1 RB RUBIDIUM ION × 2 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;293 K;AMMONIUM SULPHATE, RUBIDIUM ACETATE, PEGMME 2000, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.29 Å R-free 0.280
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 24–146 Not recorded Coagulation factor IX/X-binding protein A chain × 2 (Q7LZ71) CL CHLORIDE ION × 2 RB RUBIDIUM ION × 4 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;293 K;AMMONIUM SULPHATE, RUBIDIUM ACETATE, PEGMME 2000, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.29 Å R-free 0.280

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 9 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

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 1x2w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1x2w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1x2w
Deposition date deposition_date2005-04-26
Structure title titleCrystal Structure of Apo-Habu IX-bp at pH 4.6
Keywords keywordsHETERODIMER, DOMAIN SWAPPING, C-TYPE LECTIN-LIKE PROTEIN, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.96
Radius of gyration Rg (electron density) rg_electron21.42
Forward intensity I(0) i016147200.00
Molecular weight molecular_weight29376.0 kDa
Excluded volume excluded_volume36051 ų
Envelope volume envelope_volume42029 ų
Hydration-shell volume shell_volume17503 ų
Envelope diameter envelope_diameter80.8
Shell Rg shell_rg26.63
Envelope Rg envelope_rg21.73
Shape Rg shape_rg21.39
Total Rg total_rg22.19
Total atoms total_atoms2055
Residues n_residues252
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 dmax80.8
Rg (real space) rg_real22.19
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real1.6150e+07
I(0) uncertainty (real space) i0_real_error2.2070e+05
Rg (reciprocal space) rg_reciprocal22.15
I(0) (reciprocal space) i0_reciprocal16150000.0000
Solution quality estimate total_estimate0.7703
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.5
Skewness Skewness skewness0.558
Kurtosis Kurtosis kurtosis-0.266
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5987000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.505; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.493; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1x2wa_
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_idd1x2wb_
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

CATH v4.4 (2 domains)

Domain ID domain_id1x2wA00
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_id1x2wB00
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 (1)

9. Files and Curves (10)