1ffm

THE FIRST EGF-LIKE DOMAIN FROM HUMAN BLOOD COAGULATION FVII (FUCOSYLATED AT SER-60), NMR, MINIMIZED AVERAGE STRUCTURE

Method: SOLUTION NMR Dmax: 51.5 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 (RESIDUES 45-87; 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 1ffm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ffm
Deposition date deposition_date1999-02-19
Structure title titleTHE FIRST EGF-LIKE DOMAIN FROM HUMAN BLOOD COAGULATION FVII (FUCOSYLATED AT SER-60), NMR, MINIMIZED AVERAGE STRUCTURE
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_guinier12.99
Radius of gyration Rg (electron density) rg_electron12.24
Forward intensity I(0) i0804743.00
Molecular weight molecular_weight5017.0 kDa
Excluded volume excluded_volume5884 ų
Envelope volume envelope_volume7499 ų
Hydration-shell volume shell_volume6104 ų
Envelope diameter envelope_diameter50.3
Shell Rg shell_rg16.14
Envelope Rg envelope_rg13.00
Shape Rg shape_rg12.29
Total Rg total_rg13.13
Total atoms total_atoms645
Residues n_residues46
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 dmax51.5
Rg (real space) rg_real13.23
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real8.0470e+05
I(0) uncertainty (real space) i0_real_error9.7610e+03
Rg (reciprocal space) rg_reciprocal13.22
I(0) (reciprocal space) i0_reciprocal804700.0000
Solution quality estimate total_estimate0.7270
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary12.4
Skewness Skewness skewness0.766
Kurtosis Kurtosis kurtosis0.376
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha156400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.448; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.186; Smooth: 0.918

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_idd1ffma_
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_id1ffmA00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology25 — Laminin
Homologous superfamily homologous superfamily10 — Laminin

8. Citations (1)

9. Files and Curves (10)