2kpl

MAGI-1 PDZ1 / E6CT

Method: SOLUTION NMR Dmax: 63.2 Å Quality: REASONABLE

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

Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1

Homo sapiens

UniProt Q96QZ7

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 455–580 Fragment:UNP residues 455-580 Protein E6 × 1 (P03126) SOLUTION NMR NMR measurement conditions:pH 6.8;295 K;Pressure ambient NMR sample composition:0.2-0.6mM MAGI-1 PDZ1-1, 0.02-0.10mM sodium phosphate-2, 50mM sodium chloride-3, 2mM DTT-4, 0.6-1.8mM E6CT-5, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.2-0.6mM [U-15N] MAGI-1 PDZ1-6, 0.02-0.10mM sodium phosphate-7, 50mM sodium chloride-8, 2mM DTT-9, 0.6-1.8mM E6CT-10, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.2-0.6mM [U-100% 13C; U-100% 15N] MAGI-1 PDZ1-11, 0.02-0.10mM sodium phosphate-12, 50mM sodium chloride-13, 2mM DTT-14, 0.6-1.8mM E6CT-15, 90% H2O/10% D2O | 90% H2O/10% D2O 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.

15 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MAGI1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–129; UniProt 455–580

Protein E6

Human papillomavirus type 16

UniProt P03126

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 148–157 Not recorded Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 × 1 (Q96QZ7) SOLUTION NMR NMR measurement conditions:pH 6.8;295 K;Pressure ambient NMR sample composition:0.2-0.6mM MAGI-1 PDZ1-1, 0.02-0.10mM sodium phosphate-2, 50mM sodium chloride-3, 2mM DTT-4, 0.6-1.8mM E6CT-5, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.2-0.6mM [U-15N] MAGI-1 PDZ1-6, 0.02-0.10mM sodium phosphate-7, 50mM sodium chloride-8, 2mM DTT-9, 0.6-1.8mM E6CT-10, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.2-0.6mM [U-100% 13C; U-100% 15N] MAGI-1 PDZ1-11, 0.02-0.10mM sodium phosphate-12, 50mM sodium chloride-13, 2mM DTT-14, 0.6-1.8mM E6CT-15, 90% H2O/10% D2O | 90% H2O/10% D2O 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.

21 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VE6_HPV16
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–10; UniProt 148–157

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 2kpl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2kpl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2kpl
Deposition date deposition_date2009-10-16
Structure title titleMAGI-1 PDZ1 / E6CT
Keywords keywords;PDZ domain, ATP-binding, Cell junction, Cell membrane, Membrane, Nucleotide-binding, Phosphoprotein, Tight junction, Activator, DNA-binding, Early protein, Host-virus interaction, Metal-binding, Nucleus, Oncogene, Transcription, Transcription regulation, Zinc-finger, PROTEIN BINDING-ONCOPROTEIN complex ;; PROTEIN BINDING/ONCOPROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.43
Radius of gyration Rg (electron density) rg_electron15.15
Forward intensity I(0) i01291350000.00
Molecular weight molecular_weight304610.0 kDa
Excluded volume excluded_volume381810 ų
Envelope volume envelope_volume54802 ų
Hydration-shell volume shell_volume21926 ų
Envelope diameter envelope_diameter71.5
Shell Rg shell_rg27.98
Envelope Rg envelope_rg22.11
Shape Rg shape_rg15.11
Total Rg total_rg15.58
Total atoms total_atoms43040
Residues n_residues2800
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 dmax63.2
Rg (real space) rg_real15.46
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real1.2910e+09
I(0) uncertainty (real space) i0_real_error1.5520e+07
Rg (reciprocal space) rg_reciprocal15.45
I(0) (reciprocal space) i0_reciprocal1291000000.0000
Solution quality estimate total_estimate0.7360
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.4
Skewness Skewness skewness0.551
Kurtosis Kurtosis kurtosis0.608
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha839900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.287; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.705; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2kpla1
Class classb — All beta proteins
Fold Fold foldb.36 — PDZ domain-like
Superfamily Superfamily superfamilyb.36.1 — PDZ domain-like
Family Family familyb.36.1.1 — PDZ domain
Domain ID domain_idd2kpla2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2kplA00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology42 — Pdz3 Domain
Homologous superfamily homologous superfamily10 — PDZ domain

8. Citations (1)

9. Files and Curves (10)