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1sat

CRYSTAL STRUCTURE OF THE 50 KDA METALLO PROTEASE FROM S. MARCESCENS

Method: X-RAY DIFFRACTION Dmax: 96.3 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

SERRATIA PROTEASE

OrganismNot specified

UniProt P23694

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 17–487 Not recorded ZN ZINC ION × 1 CA CALCIUM ION × 7 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.75 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.

Other PDB Difference from Current Entry 1SAT Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1AF0 SERRATIA PROTEASE IN COMPLEX WITH INHIBITOR Deposited 1997-03-20 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 17–487（471 aa）
Not recorded ZN ZINC ION × 1 CA CALCIUM ION × 7 0Z9 N-[(benzyloxy)carbonyl]-L-leucyl-N-hydroxy-L-alaninamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；0.2 M AMMONIUM SULFATE, 20%PEG 4K, PH 6.5
Resolution 1.80 Å
1SMP CRYSTAL STRUCTURE OF A COMPLEX BETWEEN SERRATIA MARCESCENS METALLO-PROTEASE AND AN INHIBITOR FROM ERWINIA CHRYSANTHEMI Deposited 1995-01-13 Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 17–487（471 aa）
Not recorded ZN ZINC ION × 1 CA CALCIUM ION × 7 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.30 Å R-free 0.247
5D7W Crystal structure of serralysin Deposited 2015-08-14 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 20–487（468 aa） Fragment：UNP residues 20-487
Mutation：P250L ZN ZINC ION × 1 CA CALCIUM ION × 7 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.3；289 K；PEG 8000,Ammonium sulfate,sodium citrate
Resolution 1.10 Å R-free 0.186

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRZN_SERMA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–471； UniProt 17–487

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 1sat

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1sat
Deposition date deposition_date1994-07-04
Structure title titleCRYSTAL STRUCTURE OF THE 50 KDA METALLO PROTEASE FROM S. MARCESCENS
Keywords keywordsPARALLEL BETA HELIX, PARALLEL BETA ROLL, HYDROLASE (SERINE PROTEASE); HYDROLASE (SERINE PROTEASE)
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier26.38 Å
Radius of gyration Rg (electron density) rg_electron26.13 Å
Forward intensity I(0) i044876600.00
Molecular weight molecular_weight50233.0 kDa
Excluded volume excluded_volume61752 ų
Envelope volume envelope_volume73203 ų
Hydration-shell volume shell_volume25015 ų
Envelope diameter envelope_diameter97.1 Å
Shell Rg shell_rg31.64 Å
Envelope Rg envelope_rg26.64 Å
Shape Rg shape_rg26.15 Å
Total Rg total_rg26.63 Å
Total atoms total_atoms3547
Residues n_residues468
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax96.3 Å
Rg (real space) rg_real26.64 Å
Rg uncertainty (real space) rg_real_error0.85 Å
I(0) (real space) i0_real4.4880e+07
I(0) uncertainty (real space) i0_real_error6.4070e+05
Rg (reciprocal space) rg_reciprocal26.56 Å
I(0) (reciprocal space) i0_reciprocal44870000.0000
Solution quality estimate total_estimate0.7968
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.7 Å
Skewness Skewness skewness0.644
Kurtosis Kurtosis kurtosis0.001
Angular range angular_range— – 0.3000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7608000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.572; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.661; Smooth: 0.976
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1sata1
Class classb — All beta proteins
Fold Fold foldb.80 — Single-stranded right-handed beta-helix
Superfamily Superfamily superfamilyb.80.7 — beta-Roll
Family Family familyb.80.7.1 — Serralysin-like metalloprotease, C-terminal domain
Domain ID domain_idd1sata2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.92 — Zincin-like
Superfamily Superfamily superfamilyd.92.1 — Metalloproteases ('zincins'), catalytic domain
Family Family familyd.92.1.6 — Serralysin-like metalloprotease, catalytic (N-terminal) domain

CATH v4.4 (2 domains)

Domain ID domain_id1satA01
Class class2 — Mainly Beta
Architecture architecture150 — 2 Solenoid
Topology topology10 — Alkaline Protease, subunit P, domain 1
Homologous superfamily homologous superfamily10 — Serralysin-like metalloprotease, C-terminal
Domain ID domain_id1satA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology390 — Collagenase (Catalytic Domain)
Homologous superfamily homologous superfamily10 — Collagenase (Catalytic Domain)
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8. Citations (2)

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9. Files and Curves (10)