1ipp

HOMING ENDONUCLEASE/DNA COMPLEX

Method: X-RAY DIFFRACTION Dmax: 77.8 Å Quality: EXCELLENT

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

INTRON-ENCODED ENDONUCLEASE I-PPOI

Physarum polycephalum

UniProt Q94702

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–DNA Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 23–185 Chain B; UniProt 23–185 Not recorded ;DNA (5'-D(*TP*TP*GP*AP*CP*TP*CP*TP*CP*TP*TP*AP*AP*GP*AP*GP*AP*GP*TP*CP*A)-3') ; × 2 CD CADMIUM ION × 4 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5.4;THE CRYSTALS WERE GROWN FROM A 2:1 MOLAR RATIO SOLUTION OF PROTEIN AND DNA SUPPLEMENTED WITH 2.5 MM EDTA AND 5 MM SPERMINE. THE COMPLEX WAS CRYSTALLIZED FROM 21 - 27% PEG 4000, 0.1 M CITRATE, PH 5.4 - 5.8; 20 MM NACL, 2 MM EDTA., VAPOR DIFFUSION Resolution 2.20 Å R-free 0.316

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.

49 other PDB entries and 50 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PPO1_PHYPO
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–163; UniProt 23–185 Author chain B; PDBConstruct 1–163; UniProt 23–185

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 1ipp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ipp
Deposition date deposition_date1998-03-19
Structure title titleHOMING ENDONUCLEASE/DNA COMPLEX
Keywords keywordsHOMING ENDONUCLEASE, INTRON, ZINC, DNA BINDING, PROTEIN FOLDING, TRANSCRIPTION/DNA, TRANSCRIPTION-DNA complex; TRANSCRIPTION/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.72
Radius of gyration Rg (electron density) rg_electron24.52
Forward intensity I(0) i056210900.00
Molecular weight molecular_weight48697.0 kDa
Excluded volume excluded_volume56478 ų
Envelope volume envelope_volume70380 ų
Hydration-shell volume shell_volume24492 ų
Envelope diameter envelope_diameter81.1
Shell Rg shell_rg31.23
Envelope Rg envelope_rg24.60
Shape Rg shape_rg24.54
Total Rg total_rg25.09
Total atoms total_atoms3350
Residues n_residues366
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 dmax77.8
Rg (real space) rg_real24.76
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real5.6210e+07
I(0) uncertainty (real space) i0_real_error7.6120e+05
Rg (reciprocal space) rg_reciprocal24.75
I(0) (reciprocal space) i0_reciprocal56210000.0000
Solution quality estimate total_estimate0.9006
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary76.6
Skewness Skewness skewness0.350
Kurtosis Kurtosis kurtosis-0.486
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5432000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.937; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.963; Smooth: 0.930

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1ippa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.4 — His-Me finger endonucleases
Superfamily Superfamily superfamilyd.4.1 — His-Me finger endonucleases
Family Family familyd.4.1.3 — Intron-encoded homing endonucleases
Domain ID domain_idd1ippb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.4 — His-Me finger endonucleases
Superfamily Superfamily superfamilyd.4.1 — His-Me finger endonucleases
Family Family familyd.4.1.3 — Intron-encoded homing endonucleases

CATH v4.4 (2 domains)

Domain ID domain_id1ippA00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology75 — Homing Intron 3 (I-Ppo) Encoded Endonuclease; Chain A
Homologous superfamily homologous superfamily10 — Homing Intron 3 (I-ppo) Encoded Endonuclease; Chain A
Domain ID domain_id1ippB00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology75 — Homing Intron 3 (I-Ppo) Encoded Endonuclease; Chain A
Homologous superfamily homologous superfamily10 — Homing Intron 3 (I-ppo) Encoded Endonuclease; Chain A

8. Citations (2)

9. Files and Curves (10)