1b7y

PHENYLALANYL TRNA SYNTHETASE COMPLEXED WITH PHENYLALANINYL-ADENYLATE

Method: X-RAY DIFFRACTION Dmax: 136.1 Å Quality: GOOD

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

PROTEIN (PHENYLALANYL-TRNA SYNTHETASE)

OrganismNot specified

UniProt P27001

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 1–350 Not recorded PROTEIN (PHENYLALANYL-TRNA SYNTHETASE) × 2 (P27002) MG MAGNESIUM ION × 2 FYA ADENOSINE-5'-[PHENYLALANINOL-PHOSPHATE] × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;313 K;HANGING-DROP TECHNIQUE AT 4O C WITH (NH4)2SO4 AS PRECIPITANT. EACH DROPLET OF THE PHENYLALANYL-TRNA SYNTHETASE SOLUTION (10 microliters) AT PROTEIN CONCENTRATION OF 3 TO 5 MG PER ML IN 20 MM IMIDASOL-HCL BUFFER (PH 7.8), 1 MM MGCL2, 1 MM NAN3 AND 15% SATURATED (NH4)2SO4 IN THE SAME BUFFER. CRYSTALS APPEARED AFTER ONE TO TWO WEEKS AND GREW UP TO THE MAXIMAL DIMENSIONS OF 0.4X0.4X0.25 MM IN A FEW WEEKS, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 313K Resolution 2.50 Å R-free 0.267

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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SYFA_THETH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–350; UniProt 1–350

PROTEIN (PHENYLALANYL-TRNA SYNTHETASE)

OrganismNot specified

UniProt P27002

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 1–785 Not recorded PROTEIN (PHENYLALANYL-TRNA SYNTHETASE) × 2 (P27001) MG MAGNESIUM ION × 2 FYA ADENOSINE-5'-[PHENYLALANINOL-PHOSPHATE] × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;313 K;HANGING-DROP TECHNIQUE AT 4O C WITH (NH4)2SO4 AS PRECIPITANT. EACH DROPLET OF THE PHENYLALANYL-TRNA SYNTHETASE SOLUTION (10 microliters) AT PROTEIN CONCENTRATION OF 3 TO 5 MG PER ML IN 20 MM IMIDASOL-HCL BUFFER (PH 7.8), 1 MM MGCL2, 1 MM NAN3 AND 15% SATURATED (NH4)2SO4 IN THE SAME BUFFER. CRYSTALS APPEARED AFTER ONE TO TWO WEEKS AND GREW UP TO THE MAXIMAL DIMENSIONS OF 0.4X0.4X0.25 MM IN A FEW WEEKS, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 313K Resolution 2.50 Å R-free 0.267

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.

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

View Construct and Data Evidence
UniProt name SYFB_THETH
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–785; UniProt 1–785

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 1b7y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1b7y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1b7y
Deposition date deposition_date1999-01-26
Structure title titlePHENYLALANYL TRNA SYNTHETASE COMPLEXED WITH PHENYLALANINYL-ADENYLATE
Keywords keywordsENZYME, TRNA SYNTHETASE, ALPHA/BETA HOMODIMER, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.10
Radius of gyration Rg (electron density) rg_electron38.26
Forward intensity I(0) i0193369000.00
Molecular weight molecular_weight115820.0 kDa
Excluded volume excluded_volume146410 ų
Envelope volume envelope_volume195270 ų
Hydration-shell volume shell_volume44754 ų
Envelope diameter envelope_diameter141.9
Shell Rg shell_rg41.42
Envelope Rg envelope_rg38.87
Shape Rg shape_rg38.25
Total Rg total_rg38.50
Total atoms total_atoms8200
Residues n_residues1040
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 dmax136.1
Rg (real space) rg_real38.54
Rg uncertainty (real space) rg_real_error1.26
I(0) (real space) i0_real1.9340e+08
I(0) uncertainty (real space) i0_real_error3.6110e+06
Rg (reciprocal space) rg_reciprocal38.27
I(0) (reciprocal space) i0_reciprocal193300000.0000
Solution quality estimate total_estimate0.8105
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary36.5
Skewness Skewness skewness0.629
Kurtosis Kurtosis kurtosis0.038
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha41160000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.710; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.835; Smooth: 0.566

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (7 domains)

Domain ID domain_idd1b7ya_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.104 — Class II aaRS and biotin synthetases
Superfamily Superfamily superfamilyd.104.1 — Class II aaRS and biotin synthetases
Family Family familyd.104.1.1 — Class II aminoacyl-tRNA synthetase (aaRS)-like, catalytic domain
Domain ID domain_idd1b7yb1
Class classa — All alpha proteins
Fold Fold folda.6 — Putative DNA-binding domain
Superfamily Superfamily superfamilya.6.1 — Putative DNA-binding domain
Family Family familya.6.1.1 — Domains B1 and B5 of PheRS-beta, PheT
Domain ID domain_idd1b7yb2
Class classa — All alpha proteins
Fold Fold folda.6 — Putative DNA-binding domain
Superfamily Superfamily superfamilya.6.1 — Putative DNA-binding domain
Family Family familya.6.1.1 — Domains B1 and B5 of PheRS-beta, PheT
Domain ID domain_idd1b7yb3
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.4 — Nucleic acid-binding proteins
Family Family familyb.40.4.4 — Myf domain
Domain ID domain_idd1b7yb4
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.13 — Anticodon-binding domain of PheRS
Family Family familyd.58.13.1 — Anticodon-binding domain of PheRS
Domain ID domain_idd1b7yb5
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.104 — Class II aaRS and biotin synthetases
Superfamily Superfamily superfamilyd.104.1 — Class II aaRS and biotin synthetases
Family Family familyd.104.1.1 — Class II aminoacyl-tRNA synthetase (aaRS)-like, catalytic domain
Domain ID domain_idd1b7yb6
Class classb — All beta proteins
Fold Fold foldb.153 — PheT/TilS domain
Superfamily Superfamily superfamilyb.153.1 — PheT/TilS domain
Family Family familyb.153.1.1 — B3/B4 domain of PheRS, PheT

CATH v4.4 (7 domains)

Domain ID domain_id1b7yA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology930 — BirA Bifunctional Protein; domain 2
Homologous superfamily homologous superfamily10 — Bira Bifunctional Protein; Domain 2
Domain ID domain_id1b7yB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology56 — Phenylalanyl-tRNA Synthetase; Chain B, domain 1
Homologous superfamily homologous superfamily10
Domain ID domain_id1b7yB02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily140 — Nucleic acid-binding proteins
Domain ID domain_id1b7yB03
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology40 — Phenylalanyl-tRNA Synthetase; Chain B, domain 3
Homologous superfamily homologous superfamily10 — Phenylalanyl-trna Synthetase, Chain B, domain 3
Domain ID domain_id1b7yB04
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology56 — Phenylalanyl-tRNA Synthetase; Chain B, domain 1
Homologous superfamily homologous superfamily10
Domain ID domain_id1b7yB05
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology930 — BirA Bifunctional Protein; domain 2
Homologous superfamily homologous superfamily10 — Bira Bifunctional Protein; Domain 2
Domain ID domain_id1b7yB06
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily380 — Ferrodoxin-fold anticodon-binding domain

8. Citations (3)

9. Files and Curves (10)