2prq

X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica

Method: X-RAY DIFFRACTION Dmax: 55.7 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 CO COBALT (II) ION × 2 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;298 K;100 mM Tris pH 8.0, 100 mM KSCN, 4.5 M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 298KK Resolution 2.15 Å R-free 0.273

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 2prq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2prq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2prq
Deposition date deposition_date2007-05-04
Structure title titleX-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica
Keywords keywordsTris, peptidase, aminohydrolase, Cobalt, metalloprotease, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.96
Radius of gyration Rg (electron density) rg_electron16.80
Forward intensity I(0) i018549300.00
Molecular weight molecular_weight31629.0 kDa
Excluded volume excluded_volume38896 ų
Envelope volume envelope_volume39413 ų
Hydration-shell volume shell_volume18963 ų
Envelope diameter envelope_diameter56.2
Shell Rg shell_rg23.66
Envelope Rg envelope_rg17.07
Shape Rg shape_rg16.81
Total Rg total_rg17.65
Total atoms total_atoms2221
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 dmax55.7
Rg (real space) rg_real17.79
Rg uncertainty (real space) rg_real_error0.21
I(0) (real space) i0_real1.8550e+07
I(0) uncertainty (real space) i0_real_error1.9780e+05
Rg (reciprocal space) rg_reciprocal17.81
I(0) (reciprocal space) i0_reciprocal18550000.0000
Solution quality estimate total_estimate0.8927
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.3
Skewness Skewness skewness0.070
Kurtosis Kurtosis kurtosis-0.459
Angular range angular_range— – 0.4450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4969000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.982

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2prqa_
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_id2prqA00
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)