1grc

CRYSTAL STRUCTURE OF GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE FROM ESCHERICHIA COLI AT 3.0 ANGSTROMS RESOLUTION: A TARGET ENZYME FOR CHEMOTHERAPY

Method: X-RAY DIFFRACTION Dmax: 84.1 Å Quality: GOOD

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

GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE

Escherichia coli

UniProt P08179

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 1–212 Chain B; UniProt 1–212 Not recorded PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.00 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.

8 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PUR3_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–212; UniProt 1–212 Author chain B; PDBConstruct 1–212; UniProt 1–212

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 1grc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1grc
Deposition date deposition_date1992-07-21
Structure title titleCRYSTAL STRUCTURE OF GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE FROM ESCHERICHIA COLI AT 3.0 ANGSTROMS RESOLUTION: A TARGET ENZYME FOR CHEMOTHERAPY
Keywords keywordsTRANSFERASE(FORMYL); TRANSFERASE(FORMYL)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.40
Radius of gyration Rg (electron density) rg_electron24.89
Forward intensity I(0) i030319000.00
Molecular weight molecular_weight42031.0 kDa
Excluded volume excluded_volume52528 ų
Envelope volume envelope_volume63784 ų
Hydration-shell volume shell_volume22814 ų
Envelope diameter envelope_diameter86.0
Shell Rg shell_rg30.62
Envelope Rg envelope_rg25.38
Shape Rg shape_rg24.91
Total Rg total_rg25.48
Total atoms total_atoms2963
Residues n_residues386
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 dmax84.1
Rg (real space) rg_real25.57
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real3.0320e+07
I(0) uncertainty (real space) i0_real_error4.1560e+05
Rg (reciprocal space) rg_reciprocal25.52
I(0) (reciprocal space) i0_reciprocal30320000.0000
Solution quality estimate total_estimate0.8623
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.8
Skewness Skewness skewness0.538
Kurtosis Kurtosis kurtosis-0.257
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4373000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.795; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.923; Smooth: 0.897

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1grca_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.65 — Formyltransferase
Superfamily Superfamily superfamilyc.65.1 — Formyltransferase
Family Family familyc.65.1.1 — Formyltransferase
Domain ID domain_idd1grcb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.65 — Formyltransferase
Superfamily Superfamily superfamilyc.65.1 — Formyltransferase
Family Family familyc.65.1.1 — Formyltransferase

CATH v4.4 (2 domains)

Domain ID domain_id1grcA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily170 — Formyl transferase, N-terminal domain
Domain ID domain_id1grcB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily170 — Formyl transferase, N-terminal domain

8. Citations (3)

9. Files and Curves (10)