1a4y

RIBONUCLEASE INHIBITOR-ANGIOGENIN COMPLEX

Method: X-RAY DIFFRACTION Dmax: 103.7 Å Quality: GOOD

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

RIBONUCLEASE INHIBITOR

Homo sapiens

UniProt P13489

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–460 Chain D; UniProt 1–460 Not recorded ANGIOGENIN × 2 (P03950) X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.2;THE COMPLEX WAS CRYSTALLIZED FROM 10% PEG4000, 20MM SODIUM CITRATE (PH 4.2), 0.1 AMMONIUM SULPHATE AND 25 MM DTT. Resolution 2.00 Å R-free 0.286

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.

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

View Construct and Data Evidence
UniProt name RINI_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–460; UniProt 1–460 Author chain D; PDBConstruct 1–460; UniProt 1–460

ANGIOGENIN

Homo sapiens

UniProt P03950

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 25–147 Chain E; UniProt 25–147 Not recorded RIBONUCLEASE INHIBITOR × 2 (P13489) X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.2;THE COMPLEX WAS CRYSTALLIZED FROM 10% PEG4000, 20MM SODIUM CITRATE (PH 4.2), 0.1 AMMONIUM SULPHATE AND 25 MM DTT. Resolution 2.00 Å R-free 0.286

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.

53 other PDB entries and 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ANGI_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–123; UniProt 25–147 Author chain E; PDBConstruct 1–123; UniProt 25–147

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 1a4y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a4y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a4y
Deposition date deposition_date1998-02-08
Structure title titleRIBONUCLEASE INHIBITOR-ANGIOGENIN COMPLEX
Keywords keywords;COMPLEX (INHIBITOR-NUCLEASE), COMPLEX (RI-ANG), HYDROLASE MOLECULAR RECOGNITION, EPITOPE MAPPING, LEUCINE-RICH REPEATS, COMPLEX (INHIBITOR-NUCLEASE) complex ;; COMPLEX (INHIBITOR/NUCLEASE)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.40
Radius of gyration Rg (electron density) rg_electron31.23
Forward intensity I(0) i0274745000.00
Molecular weight molecular_weight126250.0 kDa
Excluded volume excluded_volume155830 ų
Envelope volume envelope_volume197170 ų
Hydration-shell volume shell_volume51486 ų
Envelope diameter envelope_diameter112.4
Shell Rg shell_rg39.37
Envelope Rg envelope_rg30.28
Shape Rg shape_rg31.24
Total Rg total_rg31.85
Total atoms total_atoms8806
Residues n_residues1166
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 dmax103.7
Rg (real space) rg_real32.14
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real2.7470e+08
I(0) uncertainty (real space) i0_real_error4.0190e+06
Rg (reciprocal space) rg_reciprocal32.26
I(0) (reciprocal space) i0_reciprocal274800000.0000
Solution quality estimate total_estimate0.7925
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary44.5
Skewness Skewness skewness0.109
Kurtosis Kurtosis kurtosis-0.286
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha90410000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.776; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.000

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_idd1a4ya_
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_idd1a4yb_
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_idd1a4yd_
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_idd1a4ye_
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

CATH v4.4 (4 domains)

Domain ID domain_id1a4yA00
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_id1a4yB00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology130 — P-30 Protein
Homologous superfamily homologous superfamily10 — Ribonuclease A-like domain
Domain ID domain_id1a4yD00
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_id1a4yE00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology130 — P-30 Protein
Homologous superfamily homologous superfamily10 — Ribonuclease A-like domain

8. Citations (1)

9. Files and Curves (10)