5gnv

Structure of PSD-95/MAP1A complex reveals unique target recognition mode of MAGUK GK domain

Method: X-RAY DIFFRACTION Dmax: 59.0 Å Quality: GOOD

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

Disks large homolog 4

Rattus norvegicus

UniProt P31016

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 531–713 Fragment:UNP residues 531-713 Microtubule-associated protein 1A × 1 (Q9QYR6) SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 6.5;289 K;0.2M lithium sulfate, 0.1M Bis-Tris pH 6.5 and 25%(w/v) polyethylene glycol 3350 Resolution 2.60 Å R-free 0.257

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.

40 other PDB entries and 58 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DLG4_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–189; UniProt 531–713

Microtubule-associated protein 1A

OrganismNot specified

UniProt Q9QYR6

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 1866–1891 Fragment:UNP residues 1866-1891 Disks large homolog 4 × 1 (P31016) SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 6.5;289 K;0.2M lithium sulfate, 0.1M Bis-Tris pH 6.5 and 25%(w/v) polyethylene glycol 3350 Resolution 2.60 Å R-free 0.257

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name MAP1A_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–26; UniProt 1866–1891

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 5gnv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5gnv
Deposition date deposition_date2016-07-25
Structure title titleStructure of PSD-95/MAP1A complex reveals unique target recognition mode of MAGUK GK domain
Keywords keywordsbinding-induced folding, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.44
Radius of gyration Rg (electron density) rg_electron17.25
Forward intensity I(0) i09903260.00
Molecular weight molecular_weight22370.0 kDa
Excluded volume excluded_volume27602 ų
Envelope volume envelope_volume33087 ų
Hydration-shell volume shell_volume16325 ų
Envelope diameter envelope_diameter55.5
Shell Rg shell_rg22.88
Envelope Rg envelope_rg17.24
Shape Rg shape_rg17.24
Total Rg total_rg18.15
Total atoms total_atoms1576
Residues n_residues200
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 dmax59.0
Rg (real space) rg_real18.34
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real9.9030e+06
I(0) uncertainty (real space) i0_real_error1.2270e+05
Rg (reciprocal space) rg_reciprocal18.35
I(0) (reciprocal space) i0_reciprocal9903000.0000
Solution quality estimate total_estimate0.8183
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary24.2
Skewness Skewness skewness0.123
Kurtosis Kurtosis kurtosis-0.523
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2279000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.882; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id5gnvA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)