1gto

HIGH RESOLUTION STRUCTURE OF A HYPERSTABLE HELICAL BUNDLE PROTEIN MUTANT

Method: X-RAY DIFFRACTION Dmax: 53.2 Å Quality: REASONABLE

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

ROP

Escherichia coli

UniProt P03051

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 2–62 Mutation:M1G, D30G No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.82 Å R-free 0.280
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 2–62 Chain C; UniProt 2–62 Mutation:M1G, D30G No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.82 Å R-free 0.280

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.

18 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ROP_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–62; UniProt 2–62 Author chain B; PDBConstruct 2–62; UniProt 2–62 Author chain C; PDBConstruct 2–62; UniProt 2–62

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 1gto

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1gto
Deposition date deposition_date1996-04-23
Structure title titleHIGH RESOLUTION STRUCTURE OF A HYPERSTABLE HELICAL BUNDLE PROTEIN MUTANT
Keywords keywordsTRANSCRIPTION REGULATION, TURN, HELIX PACKING, CRYSTAL CONTACTS; TRANSCRIPTION REGULATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.73
Radius of gyration Rg (electron density) rg_electron16.94
Forward intensity I(0) i08348510.00
Molecular weight molecular_weight19841.0 kDa
Excluded volume excluded_volume24291 ų
Envelope volume envelope_volume28749 ų
Hydration-shell volume shell_volume14691 ų
Envelope diameter envelope_diameter61.9
Shell Rg shell_rg22.48
Envelope Rg envelope_rg17.37
Shape Rg shape_rg16.91
Total Rg total_rg17.93
Total atoms total_atoms1388
Residues n_residues176
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 dmax53.2
Rg (real space) rg_real17.72
Rg uncertainty (real space) rg_real_error0.09
I(0) (real space) i0_real8.1290e+06
I(0) uncertainty (real space) i0_real_error7.6340e+04
Rg (reciprocal space) rg_reciprocal17.67
I(0) (reciprocal space) i0_reciprocal8349000.0000
Solution quality estimate total_estimate0.7007
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary19.9
Skewness Skewness skewness0.202
Kurtosis Kurtosis kurtosis-0.482
Angular range angular_range— – 0.4500 −1
Current regularization parameter α current_alpha9.9090
Highest regularization parameter α highest_alpha1888000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.974; Stabil: 0.927; Sysdev: 0.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.432

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1gtoa_
Class classa — All alpha proteins
Fold Fold folda.30 — ROP-like
Superfamily Superfamily superfamilya.30.1 — ROP protein
Family Family familya.30.1.1 — ROP protein
Domain ID domain_idd1gtob_
Class classa — All alpha proteins
Fold Fold folda.30 — ROP-like
Superfamily Superfamily superfamilya.30.1 — ROP protein
Family Family familya.30.1.1 — ROP protein
Domain ID domain_idd1gtoc_
Class classa — All alpha proteins
Fold Fold folda.30 — ROP-like
Superfamily Superfamily superfamilya.30.1 — ROP protein
Family Family familya.30.1.1 — ROP protein

CATH v4.4 (3 domains)

Domain ID domain_id1gtoA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily230
Domain ID domain_id1gtoB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily230
Domain ID domain_id1gtoC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily230

8. Citations (2)

9. Files and Curves (10)