5fm7

Double-heterohexameric rings of full-length Rvb1(ADP)Rvb2(ADP)

Method: X-RAY DIFFRACTION Dmax: 104.3 Å Quality: REASONABLE

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

RVB1

CHAETOMIUM THERMOPHILUM

UniProt G0RYI5

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 1–462 Not recorded RVB2 × 6 (G0RYC2) ADP ADENOSINE-5'-DIPHOSPHATE × 12 X-RAY DIFFRACTION X-ray crystallization conditions:0.1 M MES PH 6.0,1 M SUCCINATE, 1.2% MME Resolution 2.90 Å R-free 0.282

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.

10 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0RYI5_CHATD
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–464; UniProt 1–462

RVB2

CHAETOMIUM THERMOPHILUM

UniProt G0RYC2

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain B; UniProt 1–488 Not recorded RVB1 × 6 (G0RYI5) ADP ADENOSINE-5'-DIPHOSPHATE × 12 X-RAY DIFFRACTION X-ray crystallization conditions:0.1 M MES PH 6.0,1 M SUCCINATE, 1.2% MME Resolution 2.90 Å R-free 0.282

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.

10 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0RYC2_CHATD
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–490; UniProt 1–488

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 5fm7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5fm7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5fm7
Deposition date deposition_date2015-11-02
Structure title titleDouble-heterohexameric rings of full-length Rvb1(ADP)Rvb2(ADP)
Keywords keywordsATP BINDING PROTEIN; ATP BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.63
Radius of gyration Rg (electron density) rg_electron31.87
Forward intensity I(0) i0141366000.00
Molecular weight molecular_weight93270.0 kDa
Excluded volume excluded_volume116730 ų
Envelope volume envelope_volume164910 ų
Hydration-shell volume shell_volume43227 ų
Envelope diameter envelope_diameter109.7
Shell Rg shell_rg38.47
Envelope Rg envelope_rg32.35
Shape Rg shape_rg31.90
Total Rg total_rg32.38
Total atoms total_atoms6540
Residues n_residues840
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 dmax104.3
Rg (real space) rg_real32.58
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real1.4140e+08
I(0) uncertainty (real space) i0_real_error2.2800e+06
Rg (reciprocal space) rg_reciprocal32.60
I(0) (reciprocal space) i0_reciprocal141400000.0000
Solution quality estimate total_estimate0.7196
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.296
Kurtosis Kurtosis kurtosis-0.406
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18050000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.904; Stabil: 1.000; Sysdev: 0.242; Positv: 1.000; Valcen: 1.000; Smooth: 0.911

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id5fm7A01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily360 — RuvBL1 DNA/RNA binding domain
Domain ID domain_id5fm7A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily60
Domain ID domain_id5fm7B01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily360 — RuvBL1 DNA/RNA binding domain
Domain ID domain_id5fm7B02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily60

8. Citations (1)

9. Files and Curves (10)