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2bnh

PORCINE RIBONUCLEASE INHIBITOR

Method: X-RAY DIFFRACTION Dmax: 72.2 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–456 Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.30 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.

Other PDB Difference from Current Entry 2BNH Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1DFJ RIBONUCLEASE INHIBITOR COMPLEXED WITH RIBONUCLEASE A Deposited 1996-06-29 Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain I 1–456（456 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.50 Å

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 1
Chains and sequence ranges Author chain A； 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 2bnh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2bnh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2bnh
Deposition date deposition_date1996-06-29
Structure title titlePORCINE RIBONUCLEASE INHIBITOR
Keywords keywordsACETYLATION, LEUCINE-RICH REPEATS; ACETYLATION
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier26.01 Å
Radius of gyration Rg (electron density) rg_electron24.93 Å
Forward intensity I(0) i042562800.00
Molecular weight molecular_weight49044.0 kDa
Excluded volume excluded_volume60799 ų
Envelope volume envelope_volume76084 ų
Hydration-shell volume shell_volume25072 ų
Envelope diameter envelope_diameter74.4 Å
Shell Rg shell_rg32.66 Å
Envelope Rg envelope_rg24.42 Å
Shape Rg shape_rg24.94 Å
Total Rg total_rg25.70 Å
Total atoms total_atoms3414
Residues n_residues455
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 dmax72.2 Å
Rg (real space) rg_real25.90 Å
Rg uncertainty (real space) rg_real_error0.28 Å
I(0) (real space) i0_real4.2560e+07
I(0) uncertainty (real space) i0_real_error4.8070e+05
Rg (reciprocal space) rg_reciprocal25.93 Å
I(0) (reciprocal space) i0_reciprocal42560000.0000
Solution quality estimate total_estimate0.9158
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.7 Å
Skewness Skewness skewness0.066
Kurtosis Kurtosis kurtosis-0.810
Angular range angular_range— – 0.3050 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13230000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.987; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.949
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2bnha_
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 (1 domains)

Domain ID domain_id2bnhA00
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
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8. Citations (3)

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9. Files and Curves (10)