1bk7

RIBONUCLEASE MC1 FROM THE SEEDS OF BITTER GOURD

Method: X-RAY DIFFRACTION Dmax: 53.5 Å Quality: EXCELLENT

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

PROTEIN (RIBONUCLEASE MC1)

OrganismNot specified

UniProt P23540

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 1–191 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.7;PROTEN WAS CRYSTALLIZED FROM THE 1:1 MIXTURE OF 10MG/ML PROTEIN SOLUTION IN 5MM TRIS-HCL PH7.2 AND 30% PEG 6000, 0.2M NA-ACETATE, 0.1M NA-CACODYLATE PH 6.7 Resolution 1.75 Å R-free 0.241

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.

7 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RNMC_MOMCH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–190; UniProt 1–191

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 1bk7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bk7
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1bk7
Deposition date deposition_date1998-07-15
Structure title titleRIBONUCLEASE MC1 FROM THE SEEDS OF BITTER GOURD
Keywords keywordsHYDROLASE (NUCLEIC ACID, RNA), HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.42
Radius of gyration Rg (electron density) rg_electron16.23
Forward intensity I(0) i08502300.00
Molecular weight molecular_weight21212.0 kDa
Excluded volume excluded_volume26398 ų
Envelope volume envelope_volume29768 ų
Hydration-shell volume shell_volume15444 ų
Envelope diameter envelope_diameter52.8
Shell Rg shell_rg22.10
Envelope Rg envelope_rg16.43
Shape Rg shape_rg16.20
Total Rg total_rg17.29
Total atoms total_atoms1496
Residues n_residues190
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 dmax53.5
Rg (real space) rg_real17.30
Rg uncertainty (real space) rg_real_error0.23
I(0) (real space) i0_real8.5020e+06
I(0) uncertainty (real space) i0_real_error8.0110e+04
Rg (reciprocal space) rg_reciprocal17.31
I(0) (reciprocal space) i0_reciprocal8502000.0000
Solution quality estimate total_estimate0.9057
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.4
Skewness Skewness skewness0.118
Kurtosis Kurtosis kurtosis-0.474
Angular range angular_range— – 0.4550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1453000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1bk7a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.124 — Ribonuclease Rh-like
Superfamily Superfamily superfamilyd.124.1 — Ribonuclease Rh-like
Family Family familyd.124.1.1 — Ribonuclease Rh-like

CATH v4.4 (1 domains)

Domain ID domain_id1bk7A00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology730 — Ribonuclease Rh; Chain A
Homologous superfamily homologous superfamily10 — Ribonuclease T2-like

8. Citations (4)

9. Files and Curves (10)