1ssx

0.83A resolution crystal structure of alpha-lytic protease at pH 8

Method: X-RAY DIFFRACTION Dmax: 52.0 Å Quality: GOOD

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

Alpha-lytic protease

Lysobacter enzymogenes

UniProt P00778

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 200–397 Fragment:Mature protease domain (residues 200-397) SO4 SULFATE ION × 4 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;298 K;1.3M lithium sulfate, 0.02M Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 0.83 Å R-free 0.099

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.

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

View Construct and Data Evidence
UniProt name PRLA_LYSEN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–198; UniProt 200–397

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 1ssx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ssx
Deposition date deposition_date2004-03-24
Structure title title0.83A resolution crystal structure of alpha-lytic protease at pH 8
Keywords keywordsa-lytic protease, serine protease, protein folding, protein stability, packing distortion, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.36
Radius of gyration Rg (electron density) rg_electron15.12
Forward intensity I(0) i09277300.00
Molecular weight molecular_weight20437.0 kDa
Excluded volume excluded_volume24771 ų
Envelope volume envelope_volume27423 ų
Hydration-shell volume shell_volume14997 ų
Envelope diameter envelope_diameter51.9
Shell Rg shell_rg21.37
Envelope Rg envelope_rg15.46
Shape Rg shape_rg15.08
Total Rg total_rg16.23
Total atoms total_atoms2794
Residues n_residues171
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 dmax52.0
Rg (real space) rg_real16.23
Rg uncertainty (real space) rg_real_error0.21
I(0) (real space) i0_real9.2770e+06
I(0) uncertainty (real space) i0_real_error9.4250e+04
Rg (reciprocal space) rg_reciprocal16.24
I(0) (reciprocal space) i0_reciprocal9277000.0000
Solution quality estimate total_estimate0.8883
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.7
Skewness Skewness skewness0.110
Kurtosis Kurtosis kurtosis-0.420
Angular range angular_range— – 0.4850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2687000.0000
Real-space data points n_real_points79
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.854; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1ssxa_
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.47.1.1 — Prokaryotic proteases

CATH v4.4 (2 domains)

Domain ID domain_id1ssxA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1ssxA02
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)