4peq

Structure of bovine ribonuclease inhibitor complexed with bovine ribonuclease I

Method: X-RAY DIFFRACTION Dmax: 109.6 Å Quality: GOOD

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

Ribonuclease pancreatic

Bos taurus

UniProt P61823

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 27–150 Fragment:UNP residues 27-150 Ribonuclease/angiogenin inhibitor 1 × 1 (Q3SZN8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4;298 K;1:1 protein solution (20 mM HEPES-NaOH, 10 mM DTT, 2% w/v glycerol, pH 7.5) to well solution (100 mM malic acid/MES/Tris, pH 4.0, 25% PEG1500), cryoprotectant: 100 mM malic acid/MES/Tris, pH 4.0, 25% PEG1500, 15% ethylene glycol Resolution 2.21 Å R-free 0.226
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 27–150 Fragment:UNP residues 27-150 Ribonuclease/angiogenin inhibitor 1 × 1 (Q3SZN8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4;298 K;1:1 protein solution (20 mM HEPES-NaOH, 10 mM DTT, 2% w/v glycerol, pH 7.5) to well solution (100 mM malic acid/MES/Tris, pH 4.0, 25% PEG1500), cryoprotectant: 100 mM malic acid/MES/Tris, pH 4.0, 25% PEG1500, 15% ethylene glycol Resolution 2.21 Å R-free 0.226

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.

333 other PDB entries and 494 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RNAS1_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–124; UniProt 27–150 Author chain C; PDBConstruct 1–124; UniProt 27–150

Ribonuclease/angiogenin inhibitor 1

Bos taurus

UniProt Q3SZN8

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 B; UniProt 1–456 Not recorded Ribonuclease pancreatic × 1 (P61823) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4;298 K;1:1 protein solution (20 mM HEPES-NaOH, 10 mM DTT, 2% w/v glycerol, pH 7.5) to well solution (100 mM malic acid/MES/Tris, pH 4.0, 25% PEG1500), cryoprotectant: 100 mM malic acid/MES/Tris, pH 4.0, 25% PEG1500, 15% ethylene glycol Resolution 2.21 Å R-free 0.226
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–456 Not recorded Ribonuclease pancreatic × 1 (P61823) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4;298 K;1:1 protein solution (20 mM HEPES-NaOH, 10 mM DTT, 2% w/v glycerol, pH 7.5) to well solution (100 mM malic acid/MES/Tris, pH 4.0, 25% PEG1500), cryoprotectant: 100 mM malic acid/MES/Tris, pH 4.0, 25% PEG1500, 15% ethylene glycol Resolution 2.21 Å R-free 0.226

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 Q3SZN8_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–456; UniProt 1–456 Author chain D; PDBConstruct 1–456; UniProt 1–456

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 4peq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4peq
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4peq
Deposition date deposition_date2014-04-24
Structure title titleStructure of bovine ribonuclease inhibitor complexed with bovine ribonuclease I
Keywords keywordsleucine-rich repeat, protein-protein complex, HYDROLASE-HYDROLASE INHIBITOR complex; HYDROLASE/HYDROLASE INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.97
Radius of gyration Rg (electron density) rg_electron33.52
Forward intensity I(0) i0257587000.00
Molecular weight molecular_weight124560.0 kDa
Excluded volume excluded_volume154180 ų
Envelope volume envelope_volume193250 ų
Hydration-shell volume shell_volume47837 ų
Envelope diameter envelope_diameter113.7
Shell Rg shell_rg40.58
Envelope Rg envelope_rg33.20
Shape Rg shape_rg33.52
Total Rg total_rg34.02
Total atoms total_atoms8673
Residues n_residues1156
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 dmax109.6
Rg (real space) rg_real33.92
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real2.5760e+08
I(0) uncertainty (real space) i0_real_error4.8830e+06
Rg (reciprocal space) rg_reciprocal33.95
I(0) (reciprocal space) i0_reciprocal257600000.0000
Solution quality estimate total_estimate0.8895
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.0
Skewness Skewness skewness0.298
Kurtosis Kurtosis kurtosis-0.367
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha83310000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.898; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.868

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd4peqa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.5 — RNase A-like
Superfamily Superfamily superfamilyd.5.1 — RNase A-like
Family Family familyd.5.1.1 — Ribonuclease A-like
Domain ID domain_idd4peqb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Superfamily Superfamily superfamilyc.10.1 — RNI-like
Family Family familyc.10.1.1 — 28-residue LRR
Domain ID domain_idd4peqc_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.5 — RNase A-like
Superfamily Superfamily superfamilyd.5.1 — RNase A-like
Family Family familyd.5.1.1 — Ribonuclease A-like
Domain ID domain_idd4peqd_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Superfamily Superfamily superfamilyc.10.1 — RNI-like
Family Family familyc.10.1.1 — 28-residue LRR

CATH v4.4 (4 domains)

Domain ID domain_id4peqA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology130 — P-30 Protein
Homologous superfamily homologous superfamily10 — Ribonuclease A-like domain
Domain ID domain_id4peqB00
Class class3 — Alpha Beta
Architecture architecture80 — Alpha-Beta Horseshoe
Topology topology10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Homologous superfamily homologous superfamily10 — Ribonuclease Inhibitor
Domain ID domain_id4peqC00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology130 — P-30 Protein
Homologous superfamily homologous superfamily10 — Ribonuclease A-like domain
Domain ID domain_id4peqD00
Class class3 — Alpha Beta
Architecture architecture80 — Alpha-Beta Horseshoe
Topology topology10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Homologous superfamily homologous superfamily10 — Ribonuclease Inhibitor

8. Citations (1)

9. Files and Curves (10)