1cpb

STRUCTURE OF CARBOXYPEPTIDASE B AT 2.8 ANGSTROMS RESOLUTION

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

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

CARBOXYPEPTIDASE B

Bos taurus

UniProt P00732

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–82 Chain B; UniProt 90–306 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.80 Å

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name CBPB1_BOVIN
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–82; UniProt 1–82 Author chain B; PDBConstruct 1–217; UniProt 90–306

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 1cpb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1cpb
Deposition date deposition_date1976-06-23
Structure title titleSTRUCTURE OF CARBOXYPEPTIDASE B AT 2.8 ANGSTROMS RESOLUTION
Keywords keywordsHYDROLASE (C-TERMINAL PEPTIDASE); HYDROLASE (C-TERMINAL PEPTIDASE)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.78
Radius of gyration Rg (electron density) rg_electron16.80
Forward intensity I(0) i018983400.00
Molecular weight molecular_weight33826.0 kDa
Excluded volume excluded_volume40950 ų
Envelope volume envelope_volume25130 ų
Hydration-shell volume shell_volume13527 ų
Envelope diameter envelope_diameter56.3
Shell Rg shell_rg21.09
Envelope Rg envelope_rg16.12
Shape Rg shape_rg16.97
Total Rg total_rg17.25
Total atoms total_atoms
Residues n_residues
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_real17.64
Rg uncertainty (real space) rg_real_error0.20
I(0) (real space) i0_real1.8980e+07
I(0) uncertainty (real space) i0_real_error2.0820e+05
Rg (reciprocal space) rg_reciprocal17.66
I(0) (reciprocal space) i0_reciprocal18980000.0000
Solution quality estimate total_estimate0.8087
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.2
Skewness Skewness skewness0.104
Kurtosis Kurtosis kurtosis-0.415
Angular range angular_range— – 0.4450 −1
Current regularization parameter α current_alpha0.0004
Highest regularization parameter α highest_alpha2803000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.840; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1cpb.1
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

8. Citations (4)

9. Files and Curves (10)