← Back to search
1af0

SERRATIA PROTEASE IN COMPLEX WITH INHIBITOR

Method: X-RAY DIFFRACTION Dmax: 95.7 Å Quality: GOOD
▼

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 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

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 1AF0 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1SAT CRYSTAL STRUCTURE OF THE 50 KDA METALLO PROTEASE FROM S. MARCESCENS Deposited 1994-07-04 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 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.75 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 ligand/ion Different experimental conditions 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 1af0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1af0
Download Download
▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id1af0
Deposition date deposition_date1997-03-20
Structure title titleSERRATIA PROTEASE IN COMPLEX WITH INHIBITOR
Keywords keywordsMETALLOPROTEASE, SERRALYSIN, HYDROLASE-HYDROLASE INHIBITOR complex; HYDROLASE/HYDROLASE INHIBITOR
Experimental Method methodX-RAY DIFFRACTION
▼

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

Radius of gyration Rg (Guinier) rg_guinier26.29 Å
Radius of gyration Rg (electron density) rg_electron26.15 Å
Forward intensity I(0) i082145500.00
Molecular weight molecular_weight47312.0 kDa
Excluded volume excluded_volume45487 ų
Envelope volume envelope_volume73649 ų
Hydration-shell volume shell_volume25125 ų
Envelope diameter envelope_diameter97.1 Å
Shell Rg shell_rg31.64 Å
Envelope Rg envelope_rg26.64 Å
Shape Rg shape_rg26.17 Å
Total Rg total_rg26.54 Å
Total atoms total_atoms3574
Residues n_residues470
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
▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax95.7 Å
Rg (real space) rg_real26.56 Å
Rg uncertainty (real space) rg_real_error0.90 Å
I(0) (real space) i0_real8.2150e+07
I(0) uncertainty (real space) i0_real_error1.1520e+06
Rg (reciprocal space) rg_reciprocal26.48 Å
I(0) (reciprocal space) i0_reciprocal82140000.0000
Solution quality estimate total_estimate0.7956
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary25.5 Å
Skewness Skewness skewness0.640
Kurtosis Kurtosis kurtosis-0.037
Angular range angular_range— – 0.3000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11430000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.577; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.626; Smooth: 0.983
▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (5)

▼

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1af0a1
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_idd1af0a2
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_id1af0A01
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_id1af0A02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology390 — Collagenase (Catalytic Domain)
Homologous superfamily homologous superfamily10 — Collagenase (Catalytic Domain)
▶

8. Citations (5)

▶

9. Files and Curves (10)