8jc5

Crystal structure of PLEKHM1 RUN domain in complex with GTP-bound Arl8b(Q75L)

Method: X-RAY DIFFRACTION Dmax: 98.4 Å Quality: GOOD

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

ADP-ribosylation factor-like protein 8B

Homo sapiens

UniProt Q9NVJ2

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 18–186 Mutation:Q75L Pleckstrin homology domain-containing family M member 1 × 1 (Q9Y4G2) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;0.2 M Lithium chloride, 0.1 M TRIS pH=7.6, 18% (w/v) PEG 8000 Resolution 2.01 Å R-free 0.201
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 18–186 Mutation:Q75L Pleckstrin homology domain-containing family M member 1 × 1 (Q9Y4G2) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;0.2 M Lithium chloride, 0.1 M TRIS pH=7.6, 18% (w/v) PEG 8000 Resolution 2.01 Å R-free 0.201

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARL8B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–169; UniProt 18–186 Author chain B; PDBConstruct 1–169; UniProt 18–186

Pleckstrin homology domain-containing family M member 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 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 10–205 Not recorded ADP-ribosylation factor-like protein 8B × 1 (Q9NVJ2) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;0.2 M Lithium chloride, 0.1 M TRIS pH=7.6, 18% (w/v) PEG 8000 Resolution 2.01 Å R-free 0.201
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 10–205 Not recorded ADP-ribosylation factor-like protein 8B × 1 (Q9NVJ2) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;0.2 M Lithium chloride, 0.1 M TRIS pH=7.6, 18% (w/v) PEG 8000 Resolution 2.01 Å R-free 0.201

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 2
Chains and sequence ranges Author chain C; PDBConstruct 1–196; UniProt 10–205 Author chain D; PDBConstruct 1–196; UniProt 10–205

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 8jc5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8jc5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8jc5
Deposition date deposition_date2023-05-10
最后修订 last_revision2024-03-27
Structure title titleCrystal structure of PLEKHM1 RUN domain in complex with GTP-bound Arl8b(Q75L)
Keywords keywordsPLEKHM1, RUN, Arl8b, GTP-bound, GTPase, Arf, 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_guinier30.05
Radius of gyration Rg (electron density) rg_electron29.03
Forward intensity I(0) i0106313000.00
Molecular weight molecular_weight81842.0 kDa
Excluded volume excluded_volume102720 ų
Envelope volume envelope_volume127230 ų
Hydration-shell volume shell_volume36383 ų
Envelope diameter envelope_diameter104.7
Shell Rg shell_rg36.38
Envelope Rg envelope_rg29.06
Shape Rg shape_rg29.03
Total Rg total_rg29.69
Total atoms total_atoms5740
Residues n_residues720
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 dmax98.4
Rg (real space) rg_real29.98
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real1.0630e+08
I(0) uncertainty (real space) i0_real_error1.6670e+06
Rg (reciprocal space) rg_reciprocal30.02
I(0) (reciprocal space) i0_reciprocal106300000.0000
Solution quality estimate total_estimate0.8942
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.4
Skewness Skewness skewness0.231
Kurtosis Kurtosis kurtosis-0.500
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha45230000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.896; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.936

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)