5b02

Structure of the prenyltransferase MoeN5 with a fusion protein tag of Sso7d

Method: X-RAY DIFFRACTION Dmax: 135.7 Å Quality: GOOD

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

MoeN5,DNA-binding protein 7d

Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

UniProt A0A010

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–260 Chain B; UniProt 1–260 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.1;298 K;0.2M Li3-citrate, 0.3M NaCl, 25% PEG 3350 Resolution 2.21 Å R-free 0.218
2 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–260 Chain D; UniProt 1–260 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.1;298 K;0.2M Li3-citrate, 0.3M NaCl, 25% PEG 3350 Resolution 2.21 Å R-free 0.218

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.

12 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A010_9ACTN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 15–274; UniProt 1–260 Author chain B; PDBConstruct 15–274; UniProt 1–260 Author chain C; PDBConstruct 15–274; UniProt 1–260 Author chain D; PDBConstruct 15–274; UniProt 1–260

MoeN5,DNA-binding protein 7d

Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

UniProt P39476

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–64 Chain B; UniProt 1–64 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.1;298 K;0.2M Li3-citrate, 0.3M NaCl, 25% PEG 3350 Resolution 2.21 Å R-free 0.218
2 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–64 Chain D; UniProt 1–64 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.1;298 K;0.2M Li3-citrate, 0.3M NaCl, 25% PEG 3350 Resolution 2.21 Å R-free 0.218

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.

19 other PDB entries and 43 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DN72_SULSO
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 280–343; UniProt 1–64 Author chain B; PDBConstruct 280–343; UniProt 1–64 Author chain C; PDBConstruct 280–343; UniProt 1–64 Author chain D; PDBConstruct 280–343; UniProt 1–64

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 5b02

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5b02
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5b02
Deposition date deposition_date2015-10-27
Structure title titleStructure of the prenyltransferase MoeN5 with a fusion protein tag of Sso7d
Keywords keywordsprenyltransferase, alpha-helical fold, DNA-binding, TRANSFERASE, DNA BINDING PROTEIN; TRANSFERASE, DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.20
Radius of gyration Rg (electron density) rg_electron38.65
Forward intensity I(0) i0275715000.00
Molecular weight molecular_weight129560.0 kDa
Excluded volume excluded_volume160340 ų
Envelope volume envelope_volume215430 ų
Hydration-shell volume shell_volume47918 ų
Envelope diameter envelope_diameter143.1
Shell Rg shell_rg42.59
Envelope Rg envelope_rg39.64
Shape Rg shape_rg38.66
Total Rg total_rg38.86
Total atoms total_atoms9088
Residues n_residues1191
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 dmax135.7
Rg (real space) rg_real38.44
Rg uncertainty (real space) rg_real_error1.26
I(0) (real space) i0_real2.7570e+08
I(0) uncertainty (real space) i0_real_error5.4980e+06
Rg (reciprocal space) rg_reciprocal38.29
I(0) (reciprocal space) i0_reciprocal275700000.0000
Solution quality estimate total_estimate0.8499
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary39.7
Skewness Skewness skewness0.504
Kurtosis Kurtosis kurtosis-0.151
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha48320000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.761; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.914; Smooth: 0.847

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id5b02A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology600 — Farnesyl Diphosphate Synthase
Homologous superfamily homologous superfamily10 — Farnesyl Diphosphate Synthase
Domain ID domain_id5b02B01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology600 — Farnesyl Diphosphate Synthase
Homologous superfamily homologous superfamily10 — Farnesyl Diphosphate Synthase
Domain ID domain_id5b02B02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40
Domain ID domain_id5b02C00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology600 — Farnesyl Diphosphate Synthase
Homologous superfamily homologous superfamily10 — Farnesyl Diphosphate Synthase
Domain ID domain_id5b02D01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology600 — Farnesyl Diphosphate Synthase
Homologous superfamily homologous superfamily10 — Farnesyl Diphosphate Synthase
Domain ID domain_id5b02D02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40

8. Citations (1)

9. Files and Curves (10)