2nyq

Structure of Vibrio proteolyticus aminopeptidase with a bound Trp fragment of dLWCF

Method: X-RAY DIFFRACTION Dmax: 56.9 Å Quality: GOOD

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

Aminopeptidase

OrganismNot specified

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 107–405 Fragment:Bacterial leucyl aminopeptidase, residues 97-405 Tetrapeptide × 1 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;296 K;5 d., 10/100/100 mM KSCN, 0.4/4.5/4.5 M NaCl, 10/100 mM Tris/100 mM Tricine, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 296K Resolution 2.50 Å R-free 0.256

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 1–299; UniProt 107–405

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 2nyq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2nyq
Deposition date deposition_date2006-11-21
Structure title titleStructure of Vibrio proteolyticus aminopeptidase with a bound Trp fragment of dLWCF
Keywords keywordsTrp, VpAP, non-covalent, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.34
Radius of gyration Rg (electron density) rg_electron17.17
Forward intensity I(0) i018664400.00
Molecular weight molecular_weight31690.0 kDa
Excluded volume excluded_volume38979 ų
Envelope volume envelope_volume41681 ų
Hydration-shell volume shell_volume19634 ų
Envelope diameter envelope_diameter58.8
Shell Rg shell_rg24.12
Envelope Rg envelope_rg17.40
Shape Rg shape_rg17.17
Total Rg total_rg18.05
Total atoms total_atoms2226
Residues n_residues292
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 dmax56.9
Rg (real space) rg_real18.20
Rg uncertainty (real space) rg_real_error0.27
I(0) (real space) i0_real1.8660e+07
I(0) uncertainty (real space) i0_real_error2.1710e+05
Rg (reciprocal space) rg_reciprocal18.22
I(0) (reciprocal space) i0_reciprocal18660000.0000
Solution quality estimate total_estimate0.8943
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary55.3
Skewness Skewness skewness0.075
Kurtosis Kurtosis kurtosis-0.450
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5231000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.883; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.996

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_idd2nyqa_
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_id2nyqA00
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)