2al7

Structure Of Human ADP-Ribosylation Factor-Like 10C

Method: X-RAY DIFFRACTION Dmax: 51.1 Å Quality: GOOD

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

ADP-ribosylation factor-like 10C

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 18–184 Not recorded MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;298 K;PEG 3350 25%, Ammonium Acetate 100mM, 100mM HEPES (7.5), VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 1.85 Å R-free 0.251

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 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9NVJ2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 20–186; UniProt 18–184

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 2al7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2al7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2al7
Deposition date deposition_date2005-08-04
Structure title titleStructure Of Human ADP-Ribosylation Factor-Like 10C
Keywords keywordsTRANSPORT PROTEIN, GDP-BINDING, MEMBRANE TRAFFICKING, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.07
Radius of gyration Rg (electron density) rg_electron14.62
Forward intensity I(0) i06682360.00
Molecular weight molecular_weight18249.0 kDa
Excluded volume excluded_volume22717 ų
Envelope volume envelope_volume25457 ų
Hydration-shell volume shell_volume14380 ų
Envelope diameter envelope_diameter51.2
Shell Rg shell_rg20.91
Envelope Rg envelope_rg15.02
Shape Rg shape_rg14.62
Total Rg total_rg15.81
Total atoms total_atoms1274
Residues n_residues155
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 dmax51.1
Rg (real space) rg_real15.94
Rg uncertainty (real space) rg_real_error0.27
I(0) (real space) i0_real6.6820e+06
I(0) uncertainty (real space) i0_real_error7.6320e+04
Rg (reciprocal space) rg_reciprocal15.95
I(0) (reciprocal space) i0_reciprocal6682000.0000
Solution quality estimate total_estimate0.8060
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.3
Skewness Skewness skewness0.067
Kurtosis Kurtosis kurtosis-0.389
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1427000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.828; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2al7a1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd2al7a2
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_id2al7A00
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)