3ptl

Crystal structure of proteinase K inhibited by a lactoferrin nonapeptide, Lys-Gly-Glu-Ala-Asp-Ala-Leu-Ser-Leu-Asp at 1.3 A resolution.

Method: X-RAY DIFFRACTION Dmax: 55.1 Å Quality: GOOD

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

Proteinase K

OrganismNot specified

UniProt P06873

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 106–384 Not recorded 10-mer peptide from Lactoferrin × 1 (Q5MJE8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;295 K;tris HCl, CaCl2, NaNO3, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 1.30 Å R-free 0.250

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.

256 other PDB entries and 256 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRTK_TRIAL
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–279; UniProt 106–384

10-mer peptide from Lactoferrin

OrganismNot specified

UniProt Q5MJE8

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 405–414 Not recorded Proteinase K × 1 (P06873) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;295 K;tris HCl, CaCl2, NaNO3, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 1.30 Å R-free 0.250

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q5MJE8_SHEEP
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–10; UniProt 405–414

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 3ptl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3ptl
Deposition date deposition_date2010-12-03
Structure title titleCrystal structure of proteinase K inhibited by a lactoferrin nonapeptide, Lys-Gly-Glu-Ala-Asp-Ala-Leu-Ser-Leu-Asp at 1.3 A resolution.
Keywords keywordsHYDROLASE-INHIBITOR complex; HYDROLASE/INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.94
Radius of gyration Rg (electron density) rg_electron16.84
Forward intensity I(0) i017466400.00
Molecular weight molecular_weight29925.0 kDa
Excluded volume excluded_volume36642 ų
Envelope volume envelope_volume39641 ų
Hydration-shell volume shell_volume18988 ų
Envelope diameter envelope_diameter57.5
Shell Rg shell_rg23.80
Envelope Rg envelope_rg17.17
Shape Rg shape_rg16.86
Total Rg total_rg17.71
Total atoms total_atoms2101
Residues n_residues289
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 dmax55.1
Rg (real space) rg_real17.77
Rg uncertainty (real space) rg_real_error0.22
I(0) (real space) i0_real1.7470e+07
I(0) uncertainty (real space) i0_real_error2.0940e+05
Rg (reciprocal space) rg_reciprocal17.79
I(0) (reciprocal space) i0_reciprocal17470000.0000
Solution quality estimate total_estimate0.8939
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.8
Skewness Skewness skewness0.061
Kurtosis Kurtosis kurtosis-0.471
Angular range angular_range— – 0.4450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5513000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.889; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.977

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3ptla_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.41 — Subtilisin-like
Superfamily Superfamily superfamilyc.41.1 — Subtilisin-like
Family Family familyc.41.1.1 — Subtilases

CATH v4.4 (1 domains)

Domain ID domain_id3ptlA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily200 — Peptidase S8/S53 domain

8. Citations (1)

9. Files and Curves (10)