1ell

CADMIUM-SUBSTITUTED BOVINE PANCREATIC CARBOXYPEPTIDASE A (ALFA-FORM) AT PH 7.5 AND 0.25 M CHLORIDE IN MONOCLINIC CRYSTAL FORM.

Method: X-RAY DIFFRACTION Dmax: 59.8 Å Quality: GOOD

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

CARBOXYPEPTIDASE A

OrganismNot specified

UniProt P00730

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 P; UniProt 111–419 Fragment:ALFA-FORM CD CADMIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:MICRODIALYSIS;pH 7.5;293 K;Lithium Chloride, Tris-HNO3, Cadmium Chloride, pH 7.5, MICRODIALYSIS, temperature 293K Resolution 1.76 Å R-free 0.178

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.

29 other PDB entries and 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CBPA1_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain P; PDBConstruct 1–309; UniProt 111–419

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 1ell

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ell
Deposition date deposition_date2000-03-14
Structure title titleCADMIUM-SUBSTITUTED BOVINE PANCREATIC CARBOXYPEPTIDASE A (ALFA-FORM) AT PH 7.5 AND 0.25 M CHLORIDE IN MONOCLINIC CRYSTAL FORM.
Keywords keywordsALFA/BETA FOLD, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.47
Radius of gyration Rg (electron density) rg_electron18.11
Forward intensity I(0) i020650600.00
Molecular weight molecular_weight34613.0 kDa
Excluded volume excluded_volume43092 ų
Envelope volume envelope_volume47109 ų
Hydration-shell volume shell_volume21092 ų
Envelope diameter envelope_diameter60.9
Shell Rg shell_rg25.14
Envelope Rg envelope_rg18.33
Shape Rg shape_rg18.05
Total Rg total_rg19.21
Total atoms total_atoms2424
Residues n_residues305
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 dmax59.8
Rg (real space) rg_real19.30
Rg uncertainty (real space) rg_real_error0.24
I(0) (real space) i0_real2.0650e+07
I(0) uncertainty (real space) i0_real_error2.2310e+05
Rg (reciprocal space) rg_reciprocal19.32
I(0) (reciprocal space) i0_reciprocal20650000.0000
Solution quality estimate total_estimate0.8963
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.0
Skewness Skewness skewness0.055
Kurtosis Kurtosis kurtosis-0.469
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5906000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.891; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1ellp_
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.56.5.1 — Pancreatic carboxypeptidases

CATH v4.4 (1 domains)

Domain ID domain_id1ellP00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases

8. Citations (4)

9. Files and Curves (10)