1cfg

MEMBRANE-BINDING PEPTIDE FROM THE C2 DOMAIN OF FACTOR VIII FORMS AN AMPHIPATHIC STRUCTURE AS DETERMINED BY NMR SPECTROSCOPY

Method: SOLUTION NMR Dmax: 37.1 Å Quality: GOOD

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

COAGULATION FACTOR VIII

Homo sapiens

UniProt P00451

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 2322–2343 Not recorded No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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.

25 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FA8_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–22; UniProt 2322–2343

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 1cfg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1cfg
Deposition date deposition_date1994-11-10
Structure title titleMEMBRANE-BINDING PEPTIDE FROM THE C2 DOMAIN OF FACTOR VIII FORMS AN AMPHIPATHIC STRUCTURE AS DETERMINED BY NMR SPECTROSCOPY
Keywords keywordsCOAGULATION FACTOR; COAGULATION FACTOR
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier10.78
Radius of gyration Rg (electron density) rg_electron11.26
Forward intensity I(0) i041196400.00
Molecular weight molecular_weight54986.0 kDa
Excluded volume excluded_volume69735 ų
Envelope volume envelope_volume10222 ų
Hydration-shell volume shell_volume7189 ų
Envelope diameter envelope_diameter45.2
Shell Rg shell_rg17.37
Envelope Rg envelope_rg14.00
Shape Rg shape_rg11.15
Total Rg total_rg11.94
Total atoms total_atoms3880
Residues n_residues440
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 dmax37.1
Rg (real space) rg_real11.01
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real4.1200e+07
I(0) uncertainty (real space) i0_real_error4.1170e+05
Rg (reciprocal space) rg_reciprocal11.00
I(0) (reciprocal space) i0_reciprocal41200000.0000
Solution quality estimate total_estimate0.7754
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary8.0
Skewness Skewness skewness0.529
Kurtosis Kurtosis kurtosis-0.526
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4808.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.687; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.157; Smooth: 0.860

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1cfga_
Class classj — Peptides
Fold Fold foldj.13 — Coagulation factor VIII, membrane-binding peptide
Superfamily Superfamily superfamilyj.13.1 — Coagulation factor VIII, membrane-binding peptide
Family Family familyj.13.1.1 — Coagulation factor VIII, membrane-binding peptide

8. Citations (1)

9. Files and Curves (10)