2pf2

THE CA+2 ION AND MEMBRANE BINDING STRUCTURE OF THE GLA DOMAIN OF CA-PROTHROMBIN FRAGMENT 1

Method: X-RAY DIFFRACTION Dmax: 69.3 Å Quality: GOOD

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

PROTHROMBIN FRAGMENT 1

Bos taurus

UniProt P00735

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 44–199 Non-standard monomer:Yes (specific site not provided by mmCIF) CA CALCIUM ION × 7 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.20 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.

30 other PDB entries and 55 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name THRB_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–156; UniProt 44–199

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 2pf2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2pf2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2pf2
Deposition date deposition_date1991-12-08
Structure title titleTHE CA+2 ION AND MEMBRANE BINDING STRUCTURE OF THE GLA DOMAIN OF CA-PROTHROMBIN FRAGMENT 1
Keywords keywordsHYDROLASE(SERINE PROTEASE); HYDROLASE(SERINE PROTEASE)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.82
Radius of gyration Rg (electron density) rg_electron17.69
Forward intensity I(0) i06557740.00
Molecular weight molecular_weight17003.0 kDa
Excluded volume excluded_volume20499 ų
Envelope volume envelope_volume23709 ų
Hydration-shell volume shell_volume12309 ų
Envelope diameter envelope_diameter69.4
Shell Rg shell_rg22.19
Envelope Rg envelope_rg18.02
Shape Rg shape_rg17.65
Total Rg total_rg18.52
Total atoms total_atoms1173
Residues n_residues136
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 dmax69.3
Rg (real space) rg_real17.96
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real6.5580e+06
I(0) uncertainty (real space) i0_real_error9.2080e+04
Rg (reciprocal space) rg_reciprocal17.94
I(0) (reciprocal space) i0_reciprocal6558000.0000
Solution quality estimate total_estimate0.7825
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.8
Skewness Skewness skewness0.502
Kurtosis Kurtosis kurtosis-0.224
Angular range angular_range— – 0.4450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1275000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.552; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.513; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2pf2a1
Class classg — Small proteins
Fold Fold foldg.14 — Kringle-like
Superfamily Superfamily superfamilyg.14.1 — Kringle-like
Family Family familyg.14.1.1 — Kringle modules
Domain ID domain_idd2pf2a2
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 (1 domains)

Domain ID domain_id2pf2A00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology20 — Plasminogen Kringle 4
Homologous superfamily homologous superfamily10 — Plasminogen Kringle 4

8. Citations (3)

9. Files and Curves (10)