1a6f

RNASE P PROTEIN FROM BACILLUS SUBTILIS

Method: X-RAY DIFFRACTION Dmax: 46.3 Å Quality: GOOD

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

RIBONUCLEASE P PROTEIN

Bacillus subtilis

UniProt P25814

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 2–116 Mutation:ALA 2, HIS 3, LEU 4 ARE INSERTED BETWEEN MET 1 AND LYS 2 ZN ZINC ION × 2 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;pH 6.5 Resolution 2.60 Å R-free 0.317
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–116 Mutation:ALA 2, HIS 3, LEU 4 ARE INSERTED BETWEEN MET 1 AND LYS 2 ZN ZINC ION × 4 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;pH 6.5 Resolution 2.60 Å R-free 0.317

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name RNPA_BACSU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–119; UniProt 2–116

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 1a6f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a6f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a6f
Deposition date deposition_date1998-02-24
Structure title titleRNASE P PROTEIN FROM BACILLUS SUBTILIS
Keywords keywordsENDONUCLEASE, RNASE, SUBUNIT; ENDONUCLEASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.16
Radius of gyration Rg (electron density) rg_electron13.53
Forward intensity I(0) i03819400.00
Molecular weight molecular_weight13698.0 kDa
Excluded volume excluded_volume17204 ų
Envelope volume envelope_volume19243 ų
Hydration-shell volume shell_volume12005 ų
Envelope diameter envelope_diameter43.8
Shell Rg shell_rg19.44
Envelope Rg envelope_rg13.85
Shape Rg shape_rg13.43
Total Rg total_rg15.07
Total atoms total_atoms957
Residues n_residues113
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 dmax46.3
Rg (real space) rg_real15.03
Rg uncertainty (real space) rg_real_error0.26
I(0) (real space) i0_real3.8190e+06
I(0) uncertainty (real space) i0_real_error4.3660e+04
Rg (reciprocal space) rg_reciprocal15.04
I(0) (reciprocal space) i0_reciprocal3819000.0000
Solution quality estimate total_estimate0.8990
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.1
Skewness Skewness skewness0.065
Kurtosis Kurtosis kurtosis-0.424
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha805800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.904; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1a6fa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.14 — Ribosomal protein S5 domain 2-like
Superfamily Superfamily superfamilyd.14.1 — Ribosomal protein S5 domain 2-like
Family Family familyd.14.1.2 — RNase P protein

CATH v4.4 (1 domains)

Domain ID domain_id1a6fA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology230 — Ribosomal Protein S5; domain 2
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)