1ff7

THE FIRST EGF-LIKE DOMAIN FROM HUMAN BLOOD COAGULATION FVII (FUCOSYLATED AT SER-60), NMR, 20 STRUCTURES

Method: SOLUTION NMR Dmax: 32.2 Å Quality: REASONABLE

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

PROTEIN (Blood Coagulation Factor VII)

Homo sapiens

UniProt P08709

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 83–125 Fragment:FIRST EGF-LIKE DOMAIN (FUCOSYLATED AT SER-60) FUC alpha-L-fucopyranose × 1 SOLUTION NMR NMR measurement conditions:pH 5.5;298 K;Ionic strength (raw mmCIF value) 400mM;Pressure 1 Resolution not provided

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.

113 other PDB entries and 123 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FA7_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–43; UniProt 83–125

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 1ff7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ff7
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1ff7
Deposition date deposition_date1999-02-19
Structure title titleTHE FIRST EGF-LIKE DOMAIN FROM HUMAN BLOOD COAGULATION FVII (FUCOSYLATED AT SER-60), NMR, 20 STRUCTURES
Keywords keywordsFACTOR VII, BLOOD COAGULATION, EGF-LIKE DOMAIN, GLYCOPROTEIN, FUCOSYLATION, O- LINKED FUCOSE, BLOOD CLOTTING; BLOOD CLOTTING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier11.80
Radius of gyration Rg (electron density) rg_electron11.96
Forward intensity I(0) i0200019000.00
Molecular weight molecular_weight100350.0 kDa
Excluded volume excluded_volume117690 ų
Envelope volume envelope_volume16324 ų
Hydration-shell volume shell_volume9762 ų
Envelope diameter envelope_diameter56.3
Shell Rg shell_rg19.79
Envelope Rg envelope_rg16.40
Shape Rg shape_rg12.01
Total Rg total_rg12.00
Total atoms total_atoms12900
Residues n_residues920
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 dmax32.2
Rg (real space) rg_real11.00
Rg uncertainty (real space) rg_real_error0.07
I(0) (real space) i0_real1.9170e+08
I(0) uncertainty (real space) i0_real_error1.6390e+06
Rg (reciprocal space) rg_reciprocal12.04
I(0) (reciprocal space) i0_reciprocal200000000.0000
Solution quality estimate total_estimate0.6721
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary10.2
Skewness Skewness skewness0.434
Kurtosis Kurtosis kurtosis-0.490
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha3.1180
Highest regularization parameter α highest_alpha43060.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.970; Stabil: 0.982; Sysdev: 0.000; Positv: 1.000; Valcen: 0.882; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1ff7a_
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.11 — EGF/Laminin
Family Family familyg.3.11.1 — EGF-type module

CATH v4.4 (1 domains)

Domain ID domain_id1ff7A00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology25 — Laminin
Homologous superfamily homologous superfamily10 — Laminin

8. Citations (1)

9. Files and Curves (10)