5dpt

Crystal structure of PLEKHM1 LIR-fused human GABARAPL1_2-117

Method: X-RAY DIFFRACTION Dmax: 67.1 Å Quality: GOOD

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

;Pleckstrin homology domain-containing family M member 1, Gamma-aminobutyric acid receptor-associated protein-like 1,Gamma-aminobutyric acid receptor-associated protein-like 1 ;

Homo sapiens

UniProt Q9H0R8

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–117 Fragment:UNP Q9Y4G2 627-638, UNP Q9H0R8 2-117 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.2;278 K;20% w/v Polyethylene glycol 3,350, 0.2 M NaCl, 8% MPD pH 7.2 Resolution 2.90 Å R-free 0.260
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 2–117 Fragment:UNP Q9Y4G2 627-638, UNP Q9H0R8 2-117 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.2;278 K;20% w/v Polyethylene glycol 3,350, 0.2 M NaCl, 8% MPD pH 7.2 Resolution 2.90 Å R-free 0.260

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.

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

View Construct and Data Evidence
UniProt name GBRL1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 17–132; UniProt 2–117 Author chain B; PDBConstruct 17–132; UniProt 2–117

;Pleckstrin homology domain-containing family M member 1, Gamma-aminobutyric acid receptor-associated protein-like 1,Gamma-aminobutyric acid receptor-associated protein-like 1 ;

Homo sapiens

UniProt Q9Y4G2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 627–638 Fragment:UNP Q9Y4G2 627-638, UNP Q9H0R8 2-117 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.2;278 K;20% w/v Polyethylene glycol 3,350, 0.2 M NaCl, 8% MPD pH 7.2 Resolution 2.90 Å R-free 0.260
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 627–638 Fragment:UNP Q9Y4G2 627-638, UNP Q9H0R8 2-117 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.2;278 K;20% w/v Polyethylene glycol 3,350, 0.2 M NaCl, 8% MPD pH 7.2 Resolution 2.90 Å R-free 0.260

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.

4 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PKHM1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–14; UniProt 627–638 Author chain B; PDBConstruct 3–14; UniProt 627–638

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 5dpt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5dpt
Deposition date deposition_date2015-09-14
Structure title titleCrystal structure of PLEKHM1 LIR-fused human GABARAPL1_2-117
Keywords keywordsAutophagy, chimeric protein, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.46
Radius of gyration Rg (electron density) rg_electron19.48
Forward intensity I(0) i012876800.00
Molecular weight molecular_weight27392.0 kDa
Excluded volume excluded_volume34444 ų
Envelope volume envelope_volume42612 ų
Hydration-shell volume shell_volume18584 ų
Envelope diameter envelope_diameter70.4
Shell Rg shell_rg25.31
Envelope Rg envelope_rg19.79
Shape Rg shape_rg19.47
Total Rg total_rg20.42
Total atoms total_atoms1949
Residues n_residues245
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 dmax67.1
Rg (real space) rg_real20.42
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real1.2880e+07
I(0) uncertainty (real space) i0_real_error1.5680e+05
Rg (reciprocal space) rg_reciprocal20.43
I(0) (reciprocal space) i0_reciprocal12880000.0000
Solution quality estimate total_estimate0.8132
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.9
Skewness Skewness skewness0.305
Kurtosis Kurtosis kurtosis-0.290
Angular range angular_range— – 0.3900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2325000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.857; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5dpta_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.0 — automated matches
Domain ID domain_idd5dptb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id5dptA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id5dptB00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

8. Citations (1)

9. Files and Curves (10)