1evw

L116A MUTANT OF THE HOMING ENDONUCLEASE I-PPOI COMPLEXED TO HOMING SITE DNA.

Method: X-RAY DIFFRACTION Dmax: 129.6 Å Quality: GOOD

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

I-PPOI HOMING ENDONUCLEASE

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 4 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 1–163 Chain B; UniProt 1–163 Mutation:L116A ;DNA (5'-D(*TP*GP*GP*CP*TP*AP*CP*CP*TP*TP*AP*A)-3') ; × 1 ;DNA (5'-D(P*GP*AP*GP*AP*GP*TP*CP*A)-3') ; × 1 ;DNA (5'-D(*TP*GP*AP*CP*TP*CP*TP*CP*TP*TP*AP*A)-3') ; × 1 ;DNA (5'-D(P*GP*GP*TP*AP*GP*CP*CP*A)-3') ; × 1 MG MAGNESIUM ION × 2 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;MPD, MES pH 6.5, NaCl, MgCl2, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.10 Å R-free 0.320
2 Protein–DNA Homooligomer Protein × 2 DNA 4 PDB declaration: hexameric(6) Consistent with all polymer counts Chain C; UniProt 1–163 Chain D; UniProt 1–163 Mutation:L116A ;DNA (5'-D(*TP*GP*GP*CP*TP*AP*CP*CP*TP*TP*AP*A)-3') ; × 1 ;DNA (5'-D(P*GP*AP*GP*AP*GP*TP*CP*A)-3') ; × 1 ;DNA (5'-D(*TP*GP*AP*CP*TP*CP*TP*CP*TP*TP*AP*A)-3') ; × 1 ;DNA (5'-D(P*GP*GP*TP*AP*GP*CP*CP*A)-3') ; × 1 MG MAGNESIUM ION × 2 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;MPD, MES pH 6.5, NaCl, MgCl2, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.10 Å R-free 0.320

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 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PPO1_PHYPO
Isoform
PDB entities 5
Chains and sequence ranges Author chain A; PDBConstruct 1–163; UniProt 1–163 Author chain B; PDBConstruct 1–163; UniProt 1–163 Author chain C; PDBConstruct 1–163; UniProt 1–163 Author chain D; PDBConstruct 1–163; UniProt 1–163

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 1evw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1evw
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1evw
Deposition date deposition_date2000-04-20
Structure title titleL116A MUTANT OF THE HOMING ENDONUCLEASE I-PPOI COMPLEXED TO HOMING SITE DNA.
Keywords keywordsDNA binding B-sheets; C-terminal exchanged dimer interface; bent DNA, Hydrolase-DNA COMPLEX; Hydrolase/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.27
Radius of gyration Rg (electron density) rg_electron37.84
Forward intensity I(0) i0202593000.00
Molecular weight molecular_weight95699.0 kDa
Excluded volume excluded_volume111330 ų
Envelope volume envelope_volume161070 ų
Hydration-shell volume shell_volume37901 ų
Envelope diameter envelope_diameter132.5
Shell Rg shell_rg40.80
Envelope Rg envelope_rg36.95
Shape Rg shape_rg37.86
Total Rg total_rg37.96
Total atoms total_atoms6612
Residues n_residues728
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 dmax129.6
Rg (real space) rg_real37.54
Rg uncertainty (real space) rg_real_error1.52
I(0) (real space) i0_real2.0260e+08
I(0) uncertainty (real space) i0_real_error4.1490e+06
Rg (reciprocal space) rg_reciprocal37.38
I(0) (reciprocal space) i0_reciprocal202600000.0000
Solution quality estimate total_estimate0.8544
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.3
Skewness Skewness skewness0.439
Kurtosis Kurtosis kurtosis-0.364
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12260000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.805; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.857; Smooth: 0.830

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1evwa_
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_idd1evwb_
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_idd1evwc_
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_idd1evwd_
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 (4 domains)

Domain ID domain_id1evwA00
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_id1evwB00
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_id1evwC00
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_id1evwD00
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 (1)

9. Files and Curves (10)