3b3t

Crystal structure of the D118N mutant of the aminopeptidase from Vibrio proteolyticus

Method: X-RAY DIFFRACTION Dmax: 57.4 Å Quality: GOOD

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

Bacterial leucyl aminopeptidase

Vibrio proteolyticus

UniProt Q01693

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 107–397 Fragment:Residues 107-397 Mutation:D224N ZN ZINC ION × 2 NA SODIUM ION × 3 SCN THIOCYANATE ION × 2 ILE ISOLEUCINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;298 K;HEPES, KSCN, NaCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.17 Å R-free 0.161

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.

21 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AMPX_VIBPR
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–291; UniProt 107–397

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 3b3t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3b3t
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3b3t
Deposition date deposition_date2007-10-22
Structure title titleCrystal structure of the D118N mutant of the aminopeptidase from Vibrio proteolyticus
Keywords keywordsalpha beta, Aminopeptidase, Hydrolase, Metal-binding, Protease, Secreted, Zinc, Zymogen; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.36
Radius of gyration Rg (electron density) rg_electron17.19
Forward intensity I(0) i018813700.00
Molecular weight molecular_weight31837.0 kDa
Excluded volume excluded_volume39156 ų
Envelope volume envelope_volume41968 ų
Hydration-shell volume shell_volume19703 ų
Envelope diameter envelope_diameter58.1
Shell Rg shell_rg24.17
Envelope Rg envelope_rg17.48
Shape Rg shape_rg17.19
Total Rg total_rg18.10
Total atoms total_atoms2231
Residues n_residues291
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 dmax57.4
Rg (real space) rg_real18.22
Rg uncertainty (real space) rg_real_error0.21
I(0) (real space) i0_real1.8810e+07
I(0) uncertainty (real space) i0_real_error2.0420e+05
Rg (reciprocal space) rg_reciprocal18.24
I(0) (reciprocal space) i0_reciprocal18810000.0000
Solution quality estimate total_estimate0.8919
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.0
Skewness Skewness skewness0.082
Kurtosis Kurtosis kurtosis-0.437
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5244000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.872; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3b3ta_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.56 — Phosphorylase/hydrolase-like
Superfamily Superfamily superfamilyc.56.5 — Zn-dependent exopeptidases
Family Family familyc.56.5.4 — Bacterial dinuclear zinc exopeptidases

CATH v4.4 (1 domains)

Domain ID domain_id3b3tA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases

8. Citations (1)

9. Files and Curves (10)