1f7v

CRYSTAL STRUCTURE OF YEAST ARGINYL-TRNA SYNTHETASE COMPLEXED WITH THE TRNAARG

Method: X-RAY DIFFRACTION Dmax: 90.6 Å Quality: EXCELLENT

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

ARGINYL-TRNA SYNTHETASE

Saccharomyces cerevisiae

UniProt Q05506

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–RNA Monomer Protein × 1 RNA 1 PDB declaration: dimeric(2) Consistent with all polymer counts Chain A; UniProt 1–607 Not recorded TRNA(ARG) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;2.1 M (NH4)2SO4, hexanediol, pH 6.5, VAPOR DIFFUSION, HANGING DROP at 277K Resolution 2.90 Å R-free 0.245

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SYRC_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–607; UniProt 1–607

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 1f7v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1f7v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1f7v
Deposition date deposition_date2000-06-28
Structure title titleCRYSTAL STRUCTURE OF YEAST ARGINYL-TRNA SYNTHETASE COMPLEXED WITH THE TRNAARG
Keywords keywordstRNA-protein complex, aminoacylation, arginyl-tRNA synthetase, LIGASE-RNA COMPLEX; LIGASE/RNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.19
Radius of gyration Rg (electron density) rg_electron28.67
Forward intensity I(0) i0186161000.00
Molecular weight molecular_weight93159.0 kDa
Excluded volume excluded_volume109950 ų
Envelope volume envelope_volume141950 ų
Hydration-shell volume shell_volume40302 ų
Envelope diameter envelope_diameter96.0
Shell Rg shell_rg36.85
Envelope Rg envelope_rg28.74
Shape Rg shape_rg28.66
Total Rg total_rg29.34
Total atoms total_atoms6459
Residues n_residues667
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 dmax90.6
Rg (real space) rg_real29.08
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real1.8620e+08
I(0) uncertainty (real space) i0_real_error3.1310e+06
Rg (reciprocal space) rg_reciprocal29.13
I(0) (reciprocal space) i0_reciprocal186200000.0000
Solution quality estimate total_estimate0.9008
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.9
Skewness Skewness skewness0.214
Kurtosis Kurtosis kurtosis-0.404
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18280000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.932; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.918

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1f7va1
Class classa — All alpha proteins
Fold Fold folda.27 — Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases
Superfamily Superfamily superfamilya.27.1 — Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases
Family Family familya.27.1.1 — Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases
Domain ID domain_idd1f7va2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.26 — Adenine nucleotide alpha hydrolase-like
Superfamily Superfamily superfamilyc.26.1 — Nucleotidylyl transferase
Family Family familyc.26.1.1 — Class I aminoacyl-tRNA synthetases (RS), catalytic domain
Domain ID domain_idd1f7va3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.67 — RRF/tRNA synthetase additional domain-like
Superfamily Superfamily superfamilyd.67.2 — Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain
Family Family familyd.67.2.1 — Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain

CATH v4.4 (3 domains)

Domain ID domain_id1f7vA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily620 — HUPs
Domain ID domain_id1f7vA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology730 — Isoleucyl-tRNA Synthetase; Domain 1
Homologous superfamily homologous superfamily10 — Isoleucyl-tRNA Synthetase; Domain 1
Domain ID domain_id1f7vA03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily70 — Arginyl tRNA synthetase N-terminal domain

8. Citations (2)

9. Files and Curves (10)