5dyg

Structure of p97 N-D1 L198W mutant in complex with ADP

Method: X-RAY DIFFRACTION Dmax: 83.0 Å Quality: EXCELLENT

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

Transitional endoplasmic reticulum ATPase

Homo sapiens

UniProt P55072

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 homooligomer Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–460 Fragment:UNP residues 1-460 Mutation:L198W ADP ADENOSINE-5'-DIPHOSPHATE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;289 K;3.7 M sodium formate, pH 6.0, 8 % glycerol Resolution 2.20 Å R-free 0.258

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.

143 other PDB entries and 156 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TERA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–460; UniProt 1–460

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 5dyg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5dyg
Deposition date deposition_date2015-09-24
Structure title titleStructure of p97 N-D1 L198W mutant in complex with ADP
Keywords keywordsVCP, AAA ATPase, hydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.53
Radius of gyration Rg (electron density) rg_electron24.71
Forward intensity I(0) i043580600.00
Molecular weight molecular_weight50309.0 kDa
Excluded volume excluded_volume62831 ų
Envelope volume envelope_volume79374 ų
Hydration-shell volume shell_volume26852 ų
Envelope diameter envelope_diameter84.8
Shell Rg shell_rg31.68
Envelope Rg envelope_rg24.91
Shape Rg shape_rg24.71
Total Rg total_rg25.51
Total atoms total_atoms3528
Residues n_residues446
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 dmax83.0
Rg (real space) rg_real25.45
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real4.3580e+07
I(0) uncertainty (real space) i0_real_error5.9690e+05
Rg (reciprocal space) rg_reciprocal25.48
I(0) (reciprocal space) i0_reciprocal43580000.0000
Solution quality estimate total_estimate0.9007
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.1
Skewness Skewness skewness0.213
Kurtosis Kurtosis kurtosis-0.483
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8975000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.909; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.978

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd5dyga1
Class classb — All beta proteins
Fold Fold foldb.52 — Double psi beta-barrel
Superfamily Superfamily superfamilyb.52.2 — ADC-like
Family Family familyb.52.2.3 — Cdc48 N-terminal domain-like
Domain ID domain_idd5dyga2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.31 — Cdc48 domain 2-like
Superfamily Superfamily superfamilyd.31.1 — Cdc48 domain 2-like
Family Family familyd.31.1.1 — Cdc48 domain 2-like
Domain ID domain_idd5dyga3
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.37.1.20 — Extended AAA-ATPase domain

CATH v4.4 (4 domains)

Domain ID domain_id5dygA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology40 — Barwin-like endoglucanases
Homologous superfamily homologous superfamily20
Domain ID domain_id5dygA02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology330 — Vcp-like ATPase; Chain A, domain 2
Homologous superfamily homologous superfamily10
Domain ID domain_id5dygA03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id5dygA04
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily60

8. Citations (1)

9. Files and Curves (10)