1dfj

RIBONUCLEASE INHIBITOR COMPLEXED WITH RIBONUCLEASE A

Method: X-RAY DIFFRACTION Dmax: 75.4 Å Quality: EXCELLENT

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

RIBONUCLEASE A

OrganismNot specified

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 E; UniProt 27–150 Not recorded RIBONUCLEASE INHIBITOR × 1 (P10775) SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.50 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.

333 other PDB entries and 495 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 E; PDBConstruct 1–124; UniProt 27–150

RIBONUCLEASE INHIBITOR

OrganismNot specified

UniProt P10775

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 I; UniProt 1–456 Non-standard monomer:Yes (specific site not provided by mmCIF) RIBONUCLEASE A × 1 (P61823) SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.50 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RINI_PIG
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 2–457; 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 1dfj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1dfj
Deposition date deposition_date1996-06-29
Structure title titleRIBONUCLEASE INHIBITOR COMPLEXED WITH RIBONUCLEASE A
Keywords keywordsCOMPLEX (RIBONUCLEASE-INHIBITOR), RIBONUCLEASE, HYDROLASE, LEUCINE-RICH REPEATS, COMPLEX (ENDONUCLEASE-INHIBITOR) COMPLEX; COMPLEX (ENDONUCLEASE/INHIBITOR)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.45
Radius of gyration Rg (electron density) rg_electron25.55
Forward intensity I(0) i071549200.00
Molecular weight molecular_weight62835.0 kDa
Excluded volume excluded_volume77443 ų
Envelope volume envelope_volume95099 ų
Hydration-shell volume shell_volume30661 ų
Envelope diameter envelope_diameter77.5
Shell Rg shell_rg33.10
Envelope Rg envelope_rg25.24
Shape Rg shape_rg25.57
Total Rg total_rg26.27
Total atoms total_atoms4370
Residues n_residues580
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 dmax75.4
Rg (real space) rg_real26.31
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real7.1550e+07
I(0) uncertainty (real space) i0_real_error9.6310e+05
Rg (reciprocal space) rg_reciprocal26.35
I(0) (reciprocal space) i0_reciprocal71550000.0000
Solution quality estimate total_estimate0.9068
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary37.7
Skewness Skewness skewness0.104
Kurtosis Kurtosis kurtosis-0.695
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17510000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.983; Stabil: 0.979; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.900

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1dfje_
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_idd1dfji_
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 (2 domains)

Domain ID domain_id1dfjE00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology130 — P-30 Protein
Homologous superfamily homologous superfamily10 — Ribonuclease A-like domain
Domain ID domain_id1dfjI00
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 (3)

9. Files and Curves (10)