1bbr

THE STRUCTURE OF RESIDUES 7-16 OF THE A ALPHA CHAIN OF HUMAN FIBRINOGEN BOUND TO BOVINE THROMBIN AT 2.3 ANGSTROMS RESOLUTION

Method: X-RAY DIFFRACTION Dmax: 111.0 Å Quality: GOOD

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

EPSILON-THROMBIN

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 517–625 Chain H; UniProt 367–516 Chain L; UniProt 318–366 Not recorded FIBRINOGEN ALPHA/ALPHA-E CHAIN PRECURSOR × 1 (P02671) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.30 Å
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain J; UniProt 318–366 Chain K; UniProt 367–625 Not recorded FIBRINOGEN ALPHA/ALPHA-E CHAIN PRECURSOR × 1 (P02671) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.30 Å
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain M; UniProt 318–366 Chain N; UniProt 367–625 Not recorded FIBRINOGEN ALPHA/ALPHA-E CHAIN PRECURSOR × 1 (P02671) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.30 Å
4 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain J; UniProt 318–366 Chain K; UniProt 367–625 Chain M; UniProt 318–366 Chain N; UniProt 367–625 Not recorded FIBRINOGEN ALPHA/ALPHA-E CHAIN PRECURSOR × 2 (P02671) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.30 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 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name THRB_BOVIN
Isoform
PDB entities 1, 2, 3, 5
Chains and sequence ranges Author chain J; PDBConstruct 1–49; UniProt 318–366 Author chain L; PDBConstruct 1–49; UniProt 318–366 Author chain M; PDBConstruct 1–49; UniProt 318–366 Author chain H; PDBConstruct 1–149; UniProt 367–516 Author chain E; PDBConstruct 1–109; UniProt 517–625 Author chain K; PDBConstruct 1–259; UniProt 367–625 Author chain N; PDBConstruct 1–259; UniProt 367–625

FIBRINOGEN ALPHA/ALPHA-E CHAIN PRECURSOR

Homo sapiens

UniProt P02671

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 F; UniProt 26–35 Non-standard monomer:Yes (specific site not provided by mmCIF) EPSILON-THROMBIN × 1 (P00735) EPSILON-THROMBIN × 1 (P00735) EPSILON-THROMBIN × 1 (P00735) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.30 Å
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain G; UniProt 26–35 Non-standard monomer:Yes (specific site not provided by mmCIF) EPSILON-THROMBIN × 1 (P00735) EPSILON-THROMBIN × 1 (P00735) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.30 Å
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain I; UniProt 26–35 Non-standard monomer:Yes (specific site not provided by mmCIF) EPSILON-THROMBIN × 1 (P00735) EPSILON-THROMBIN × 1 (P00735) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.30 Å
4 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain G; UniProt 26–35 Chain I; UniProt 26–35 Non-standard monomer:Yes (specific site not provided by mmCIF) EPSILON-THROMBIN × 2 (P00735) EPSILON-THROMBIN × 2 (P00735) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.30 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.

36 other PDB entries and 66 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIBA_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 2–11; UniProt 26–35 Author chain G; PDBConstruct 2–11; UniProt 26–35 Author chain I; PDBConstruct 2–11; UniProt 26–35

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 1bbr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1bbr
Deposition date deposition_date1992-04-27
Structure title titleTHE STRUCTURE OF RESIDUES 7-16 OF THE A ALPHA CHAIN OF HUMAN FIBRINOGEN BOUND TO BOVINE THROMBIN AT 2.3 ANGSTROMS RESOLUTION
Keywords keywordsSERINE PROTEASE; SERINE PROTEASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.73
Radius of gyration Rg (electron density) rg_electron34.70
Forward intensity I(0) i0167983000.00
Molecular weight molecular_weight104770.0 kDa
Excluded volume excluded_volume131380 ų
Envelope volume envelope_volume166530 ų
Hydration-shell volume shell_volume40332 ų
Envelope diameter envelope_diameter116.5
Shell Rg shell_rg40.95
Envelope Rg envelope_rg34.33
Shape Rg shape_rg34.67
Total Rg total_rg35.23
Total atoms total_atoms7378
Residues n_residues915
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 dmax111.0
Rg (real space) rg_real34.72
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real1.6800e+08
I(0) uncertainty (real space) i0_real_error2.3310e+06
Rg (reciprocal space) rg_reciprocal34.73
I(0) (reciprocal space) i0_reciprocal168000000.0000
Solution quality estimate total_estimate0.8838
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary29.0
Skewness Skewness skewness0.206
Kurtosis Kurtosis kurtosis-0.753
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha265300000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.877; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.880

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1bbr.1
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_idd1bbr.2
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_idd1bbr.3
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

CATH v4.4 (6 domains)

Domain ID domain_id1bbrE00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1bbrH00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1bbrK01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1bbrK02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1bbrN01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1bbrN02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases

8. Citations (1)

9. Files and Curves (10)