1sap

HYPERTHERMOPHILE PROTEIN, RELAXATION MATRIX REFINEMENT STRUCTURE

Method: SOLUTION NMR Dmax: 42.0 Å Quality: GOOD

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

SAC7D

Sulfolobus acidocaldarius

UniProt P13123

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–65 Not recorded No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions Resolution not provided

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.

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

View Construct and Data Evidence
UniProt name DN71_SULAC
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–66; UniProt 1–65

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 1sap

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1sap
Deposition date deposition_date1995-04-25
Structure title titleHYPERTHERMOPHILE PROTEIN, RELAXATION MATRIX REFINEMENT STRUCTURE
Keywords keywordsDNA-BINDING PROTEIN, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.03
Radius of gyration Rg (electron density) rg_electron11.56
Forward intensity I(0) i01295890.00
Molecular weight molecular_weight7598.0 kDa
Excluded volume excluded_volume9608 ų
Envelope volume envelope_volume10792 ų
Hydration-shell volume shell_volume8346 ų
Envelope diameter envelope_diameter40.0
Shell Rg shell_rg16.67
Envelope Rg envelope_rg11.83
Shape Rg shape_rg11.50
Total Rg total_rg13.10
Total atoms total_atoms1092
Residues n_residues66
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 dmax42.0
Rg (real space) rg_real12.96
Rg uncertainty (real space) rg_real_error0.24
I(0) (real space) i0_real1.2960e+06
I(0) uncertainty (real space) i0_real_error1.4500e+04
Rg (reciprocal space) rg_reciprocal12.97
I(0) (reciprocal space) i0_reciprocal1296000.0000
Solution quality estimate total_estimate0.8835
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.0
Skewness Skewness skewness0.183
Kurtosis Kurtosis kurtosis-0.238
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha204500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.837; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.974

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1sapa_
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.13 — Chromo domain-like
Family Family familyb.34.13.1 — Histone-like proteins from archaea

CATH v4.4 (1 domains)

Domain ID domain_id1sapA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40

8. Citations (2)

9. Files and Curves (10)