1ifs

RICIN A-CHAIN (RECOMBINANT) COMPLEX WITH ADENOSINE (ADENOSINE BECOMES ADENINE IN THE COMPLEX)

Method: X-RAY DIFFRACTION Dmax: 62.5 Å Quality: GOOD

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

RICIN

Ricinus communis

UniProt P02879

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 38–298 Fragment:A CHAIN Mutation:I1M, F2V ADE ADENINE × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.00 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.

100 other PDB entries and 126 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RICI_RICCO
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–263; UniProt 38–298

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 1ifs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ifs
Deposition date deposition_date1996-07-05
Structure title titleRICIN A-CHAIN (RECOMBINANT) COMPLEX WITH ADENOSINE (ADENOSINE BECOMES ADENINE IN THE COMPLEX)
Keywords keywordsHYDROLASE, GLYCOSIDASE, TOXIN, GLYCOPROTEIN; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.30
Radius of gyration Rg (electron density) rg_electron18.02
Forward intensity I(0) i014949200.00
Molecular weight molecular_weight28981.0 kDa
Excluded volume excluded_volume36211 ų
Envelope volume envelope_volume40948 ų
Hydration-shell volume shell_volume18881 ų
Envelope diameter envelope_diameter62.4
Shell Rg shell_rg24.43
Envelope Rg envelope_rg18.27
Shape Rg shape_rg18.03
Total Rg total_rg18.93
Total atoms total_atoms2048
Residues n_residues258
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 dmax62.5
Rg (real space) rg_real19.18
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real1.4950e+07
I(0) uncertainty (real space) i0_real_error1.7010e+05
Rg (reciprocal space) rg_reciprocal19.20
I(0) (reciprocal space) i0_reciprocal14950000.0000
Solution quality estimate total_estimate0.8085
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.6
Skewness Skewness skewness0.168
Kurtosis Kurtosis kurtosis-0.351
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3362000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.836; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1ifsa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.165 — Ribosome inactivating proteins (RIP)
Superfamily Superfamily superfamilyd.165.1 — Ribosome inactivating proteins (RIP)
Family Family familyd.165.1.1 — Plant cytotoxins

CATH v4.4 (2 domains)

Domain ID domain_id1ifsA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology420 — Ricin (A subunit); domain 1
Homologous superfamily homologous superfamily10 — Ricin (A subunit), domain 1
Domain ID domain_id1ifsA02
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology470 — Ricin (A Subunit), domain 2
Homologous superfamily homologous superfamily10 — Ricin (A Subunit), domain 2

8. Citations (1)

9. Files and Curves (10)