3pmb

2.9 Angstrom crystal structure of bovine thrombin in tetragonal spacegroup

Method: X-RAY DIFFRACTION Dmax: 93.6 Å Quality: GOOD

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

Thrombin light chain

OrganismNot specified

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 336–364 Chain B; UniProt 367–625 Fragment:Bovine Thrombin Light Chain residues 336-364 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;295 K;3 microliters Bovine thrombin, 7 mg/ml in 0.01M Tris-HCl, ph 8.0, 0.05M NaCl, 0.1M sodium citrate, 20% w/v PEG3350, 15% v/v 2-propanol, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.90 Å R-free 0.301
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 336–364 Chain D; UniProt 367–625 Fragment:Bovine Thrombin Light Chain residues 336-364 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;295 K;3 microliters Bovine thrombin, 7 mg/ml in 0.01M Tris-HCl, ph 8.0, 0.05M NaCl, 0.1M sodium citrate, 20% w/v PEG3350, 15% v/v 2-propanol, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.90 Å R-free 0.301

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 54 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name THRB_BOVIN
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–29; UniProt 336–364 Author chain C; PDBConstruct 1–29; UniProt 336–364 Author chain B; PDBConstruct 1–259; UniProt 367–625 Author chain D; PDBConstruct 1–259; UniProt 367–625

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 3pmb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3pmb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3pmb
Deposition date deposition_date2010-11-16
Structure title title2.9 Angstrom crystal structure of bovine thrombin in tetragonal spacegroup
Keywords keywordsProtease, Thrombosis, Fibrinolosys, Hydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.72
Radius of gyration Rg (electron density) rg_electron28.74
Forward intensity I(0) i059358100.00
Molecular weight molecular_weight60375.0 kDa
Excluded volume excluded_volume75482 ų
Envelope volume envelope_volume95367 ų
Hydration-shell volume shell_volume27681 ų
Envelope diameter envelope_diameter97.0
Shell Rg shell_rg35.78
Envelope Rg envelope_rg28.60
Shape Rg shape_rg28.74
Total Rg total_rg29.45
Total atoms total_atoms4257
Residues n_residues468
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 dmax93.6
Rg (real space) rg_real29.82
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real5.9360e+07
I(0) uncertainty (real space) i0_real_error8.7070e+05
Rg (reciprocal space) rg_reciprocal29.78
I(0) (reciprocal space) i0_reciprocal59360000.0000
Solution quality estimate total_estimate0.8589
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary26.5
Skewness Skewness skewness0.315
Kurtosis Kurtosis kurtosis-0.771
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha45140000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.805; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.893; Smooth: 0.854

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id3pmbB01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id3pmbB02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id3pmbD01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id3pmbD02
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)