1x2t

Crystal Structure of Habu IX-bp at pH 6.5

Method: X-RAY DIFFRACTION Dmax: 90.6 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) CA CALCIUM ION × 2 1PE PENTAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 6.5;293 K;PEG 1000, PEG 8000, calcium chloride, MES, pH 6.5, MICROBATCH, temperature 293K Resolution 1.72 Å R-free 0.222
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–129 Not recorded Coagulation factor IX/factor X-binding protein B chain × 1 (P23807) CA CALCIUM ION × 2 1PE PENTAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 6.5;293 K;PEG 1000, PEG 8000, calcium chloride, MES, pH 6.5, MICROBATCH, temperature 293K Resolution 1.72 Å R-free 0.222

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 Author chain C; 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) CA CALCIUM ION × 2 1PE PENTAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 6.5;293 K;PEG 1000, PEG 8000, calcium chloride, MES, pH 6.5, MICROBATCH, temperature 293K Resolution 1.72 Å R-free 0.222
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 24–146 Not recorded Coagulation factor IX/X-binding protein A chain × 1 (Q7LZ71) CA CALCIUM ION × 2 1PE PENTAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 6.5;293 K;PEG 1000, PEG 8000, calcium chloride, MES, pH 6.5, MICROBATCH, temperature 293K Resolution 1.72 Å R-free 0.222

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 Author chain D; 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 1x2t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1x2t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1x2t
Deposition date deposition_date2005-04-26
Structure title titleCrystal Structure of Habu IX-bp at pH 6.5
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_guinier27.44
Radius of gyration Rg (electron density) rg_electron26.69
Forward intensity I(0) i060669300.00
Molecular weight molecular_weight58693.0 kDa
Excluded volume excluded_volume72211 ų
Envelope volume envelope_volume87580 ų
Hydration-shell volume shell_volume27819 ų
Envelope diameter envelope_diameter95.1
Shell Rg shell_rg33.40
Envelope Rg envelope_rg26.60
Shape Rg shape_rg26.69
Total Rg total_rg27.37
Total atoms total_atoms4124
Residues n_residues504
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 dmax90.6
Rg (real space) rg_real27.41
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real6.0670e+07
I(0) uncertainty (real space) i0_real_error8.6630e+05
Rg (reciprocal space) rg_reciprocal27.42
I(0) (reciprocal space) i0_reciprocal60670000.0000
Solution quality estimate total_estimate0.8928
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.1
Skewness Skewness skewness0.260
Kurtosis Kurtosis kurtosis-0.454
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha41470000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.878; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1x2ta_
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_idd1x2tb_
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_idd1x2tc_
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_idd1x2td_
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 (4 domains)

Domain ID domain_id1x2tA00
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_id1x2tB00
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_id1x2tC00
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_id1x2tD00
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)