2c4f

crystal structure of factor VII.stf complexed with pd0297121

Method: X-RAY DIFFRACTION Dmax: 112.5 Å Quality: GOOD

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

COAGULATION FACTOR VII PRECURSOR

OrganismNot specified

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain H; UniProt 213–466 Chain L; UniProt 61–202 Fragment:FACTOR VII HEAVY CHAIN, RESIDUES 213-466 Fragment:FACTOR VII LIGHT CHAIN, RESIDUES 61-202 Non-standard monomer:Yes (specific site not provided by mmCIF) TISSUE FACTOR PRECURSOR × 1 (P13726) TISSUE FACTOR PRECURSOR × 1 (P13726) CA CALCIUM ION × 5 GIL 2-{[6-{3-[AMINO(IMINO)METHYL]PHENOXY}-4-(DIISOPROPYLAMINO)-3,5-DIFLUOROPYRIDIN-2-YL]OXY}-5-[(ISOBUTYLAMINO)CARBONYL]BEN ZOIC ACID × 1 GLC alpha-D-glucopyranose × 1 FUC alpha-L-fucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.72 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.

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, 2
Chains and sequence ranges Author chain H; PDBConstruct 1–254; UniProt 213–466 Author chain L; PDBConstruct 1–142; UniProt 61–202

TISSUE FACTOR PRECURSOR

OrganismNot specified

UniProt P13726

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain T; UniProt 38–112 Chain U; UniProt 123–242 Fragment:FACTOR III, RESIDUES 38-112 Fragment:FACTOR III, RESIDUES 123-242 COAGULATION FACTOR VII PRECURSOR × 1 (P08709) COAGULATION FACTOR VII PRECURSOR × 1 (P08709) CA CALCIUM ION × 5 GIL 2-{[6-{3-[AMINO(IMINO)METHYL]PHENOXY}-4-(DIISOPROPYLAMINO)-3,5-DIFLUOROPYRIDIN-2-YL]OXY}-5-[(ISOBUTYLAMINO)CARBONYL]BEN ZOIC ACID × 1 GLC alpha-D-glucopyranose × 1 FUC alpha-L-fucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.72 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.

52 other PDB entries and 56 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TF_HUMAN
Isoform
PDB entities 3, 4
Chains and sequence ranges Author chain T; PDBConstruct 1–75; UniProt 38–112 Author chain U; PDBConstruct 1–116; UniProt 123–242

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 2c4f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2c4f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2c4f
Deposition date deposition_date2005-10-18
Structure title titlecrystal structure of factor VII.stf complexed with pd0297121
Keywords keywords;BLOOD COAGULATION, SERINE PROTEASE, EGF, EGF-LIKE DOMAIN, GLA, RECEPTOR ENZYME, GLYCOPROTEIN, HYDROLASE, PROTEASE, HYDROXYLATION, LIPOPROTEIN, PALMITATE, TRANSMEMBRANE ;; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.37
Radius of gyration Rg (electron density) rg_electron32.63
Forward intensity I(0) i075481300.00
Molecular weight molecular_weight67546.0 kDa
Excluded volume excluded_volume83849 ų
Envelope volume envelope_volume106520 ų
Hydration-shell volume shell_volume29533 ų
Envelope diameter envelope_diameter124.1
Shell Rg shell_rg35.95
Envelope Rg envelope_rg33.04
Shape Rg shape_rg32.58
Total Rg total_rg33.05
Total atoms total_atoms4730
Residues n_residues551
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 dmax112.5
Rg (real space) rg_real32.89
Rg uncertainty (real space) rg_real_error1.06
I(0) (real space) i0_real7.5480e+07
I(0) uncertainty (real space) i0_real_error1.2670e+06
Rg (reciprocal space) rg_reciprocal32.67
I(0) (reciprocal space) i0_reciprocal75470000.0000
Solution quality estimate total_estimate0.7867
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.6
Skewness Skewness skewness0.627
Kurtosis Kurtosis kurtosis-0.239
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10630000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.644; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.632; Smooth: 0.659

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

7. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (5 domains)

Domain ID domain_idd2c4fh1
Class classb — All beta proteins
Fold Fold foldb.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamilyb.47.1 — Trypsin-like serine proteases
Family Family familyb.47.1.2 — Eukaryotic proteases
Domain ID domain_idd2c4fl1
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
Domain ID domain_idd2c4fl2
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
Domain ID domain_idd2c4fl3
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
Domain ID domain_idd2c4fu1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.2 — Fibronectin type III
Family Family familyb.1.2.1 — Fibronectin type III

CATH v4.4 (4 domains)

Domain ID domain_id2c4fH01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id2c4fH02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id2c4fT00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2c4fU00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)