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1o6x

NMR solution structure of the activation domain of human procarboxypeptidase A2

Method: SOLUTION NMR Dmax: 40.5 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PROCARBOXYPEPTIDASE A2

HOMO SAPIENS

UniProt P48052

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 17–94 Fragment：ACTIVATION DOMAIN, RESIDUES 17-94 No other associated polymer SOLUTION NMR NMR measurement conditions：pH 7；298 K；Ionic strength (raw mmCIF value) 50MM PHOSPHATE Resolution not provided

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 1O6X Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1AYE HUMAN PROCARBOXYPEPTIDASE A2 Deposited 1997-11-03 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 17–417（401 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；pH 8.0
Resolution 1.80 Å R-free 0.222
1DTD CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE LEECH CARBOXYPEPTIDASE INHIBITOR AND THE HUMAN CARBOXYPEPTIDASE A2 (LCI-CPA2) Deposited 2000-01-12 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 116–417（302 aa）
Not recorded ZN ZINC ION × 1 GLU GLUTAMIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；298 K；ammonium phosphate, sodium citrate, pH 7.5, VAPOR DIFFUSION, temperature 298.0K
Resolution 1.65 Å R-free 0.234

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CPB2_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 4–81； UniProt 17–94

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 1o6x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1o6x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1o6x
Deposition date deposition_date2002-10-17
Structure title titleNMR solution structure of the activation domain of human procarboxypeptidase A2
Keywords keywordsACTIVATION DOMAIN, HYDROLASE, CARBOXYPEPTIDASE, METALLOPROTE; HYDROLASE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier14.86 Å
Radius of gyration Rg (electron density) rg_electron14.59 Å
Forward intensity I(0) i0448459000.00
Molecular weight molecular_weight183730.0 kDa
Excluded volume excluded_volume231770 ų
Envelope volume envelope_volume35579 ų
Hydration-shell volume shell_volume15143 ų
Envelope diameter envelope_diameter68.2 Å
Shell Rg shell_rg27.21 Å
Envelope Rg envelope_rg24.42 Å
Shape Rg shape_rg14.46 Å
Total Rg total_rg15.41 Å
Total atoms total_atoms25860
Residues n_residues1620
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 dmax40.5 Å
Rg (real space) rg_real13.36 Å
Rg uncertainty (real space) rg_real_error0.09 Å
I(0) (real space) i0_real4.2390e+08
I(0) uncertainty (real space) i0_real_error3.9160e+06
Rg (reciprocal space) rg_reciprocal15.24 Å
I(0) (reciprocal space) i0_reciprocal448500000.0000
Solution quality estimate total_estimate0.6258
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary15.9 Å
Skewness Skewness skewness0.445
Kurtosis Kurtosis kurtosis0.114
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha1.8840
Highest regularization parameter α highest_alpha121400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.014; Oscil: 0.772; Stabil: 0.987; Sysdev: 0.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1o6xa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.3 — Protease propeptides/inhibitors
Family Family familyd.58.3.1 — Pancreatic carboxypeptidase, activation domain

CATH v4.4 (1 domains)

Domain ID domain_id1o6xA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily340 — Metallocarboxypeptidase-like
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8. Citations (1)

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9. Files and Curves (10)