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1dtv

NMR STRUCTURE OF THE LEECH CARBOXYPEPTIDASE INHIBITOR (LCI)

Method: SOLUTION NMR Dmax: 48.6 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

CARBOXYPEPTIDASE INHIBITOR

OrganismNot specified

UniProt P81511

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 15–81 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions：pH 6.5；298 K；Ionic strength (raw mmCIF value) 20mM Tris；Pressure ambient NMR sample composition：1 mM in 20 mM phosphate buffer, pH 6.5 | 90% H2O/10% D2O 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 1DTV Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
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 B 20–80（61 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
1ZFI Solution structure of the leech carboxypeptidase inhibitor Deposited 2005-04-20 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 16–81（66 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3.5；300 K；Ionic strength (raw mmCIF value) 20mM phosphate buffer；Pressure ambient
NMR sample composition 1mM 15N-labeled leech carboxypeptidase inhibitor; 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 1mM 15N-labeled leech carboxypeptidase inhibitor; 100% D2O | 100% D2O
Resolution not provided
1ZFL Solution structure of III-A, the major intermediate in the oxidative folding of leech carboxypeptidase inhibitor Deposited 2005-04-20 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 16–81（66 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3.5；300 K；Ionic strength (raw mmCIF value) 20mM phosphate buffer；Pressure ambient
NMR sample composition 1mM 15N-labeled III-A intermediate; 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 1mM 15N-labeled III-A intermediate; 100% D2O | 100% D2O
Resolution not provided
2ABZ Crystal structure of C19A/C43A mutant of leech carboxypeptidase inhibitor in complex with bovine carboxypeptidase A Deposited 2005-07-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain C 16–81（66 aa）
Chain D 16–81（66 aa）
Chain E 16–81（66 aa）
Chain F 16–81（66 aa）
Mutation：C19A/C43A Mutation：C19A/C43A Mutation：C19A/C43A Mutation：C19A/C43A ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；1.5M Lithium Sulfate monohydrate, 100mM Tris, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.16 Å R-free 0.234

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MCPI_HIRME
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–67； UniProt 15–81

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 1dtv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1dtv
Deposition date deposition_date2000-01-13
Structure title titleNMR STRUCTURE OF THE LEECH CARBOXYPEPTIDASE INHIBITOR (LCI)
Keywords keywordsLeech Carboxypeptidase Inhibitor, LCI, HYDROLASE INHIBITOR; HYDROLASE INHIBITOR
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier12.61 Å
Radius of gyration Rg (electron density) rg_electron11.60 Å
Forward intensity I(0) i01366630.00
Molecular weight molecular_weight7387.0 kDa
Excluded volume excluded_volume8972 ų
Envelope volume envelope_volume9863 ų
Hydration-shell volume shell_volume7732 ų
Envelope diameter envelope_diameter46.8 Å
Shell Rg shell_rg16.38 Å
Envelope Rg envelope_rg12.33 Å
Shape Rg shape_rg11.64 Å
Total Rg total_rg12.65 Å
Total atoms total_atoms974
Residues n_residues67
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 dmax48.6 Å
Rg (real space) rg_real12.66 Å
Rg uncertainty (real space) rg_real_error0.38 Å
I(0) (real space) i0_real1.3670e+06
I(0) uncertainty (real space) i0_real_error1.4390e+04
Rg (reciprocal space) rg_reciprocal12.65 Å
I(0) (reciprocal space) i0_reciprocal1367000.0000
Solution quality estimate total_estimate0.7962
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.4 Å
Skewness Skewness skewness0.536
Kurtosis Kurtosis kurtosis0.397
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha199500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.541; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.751; Smooth: 0.973
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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_idd1dtva_
Class classg — Small proteins
Fold Fold foldg.30 — Carboxypeptidase inhibitor
Superfamily Superfamily superfamilyg.30.1 — Carboxypeptidase inhibitor
Family Family familyg.30.1.1 — Carboxypeptidase inhibitor

CATH v4.4 (1 domains)

Domain ID domain_id1dtvA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1040 — Carboxypeptidase Inhibitor; Chain A
Homologous superfamily homologous superfamily10 — Carboxypeptidase inhibitor
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8. Citations (1)

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9. Files and Curves (10)