5kiw

p97 ND1-L198W in complex with VIMP

Method: X-RAY DIFFRACTION Dmax: 157.7 Å Quality: GOOD

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–460 Chain B; UniProt 1–460 Fragment:N-terminal residues 1-460 Mutation:L198W Selenoprotein S × 2 (Q9BQE4) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;288 K;0.1 M Tris, pH 8, 15 % ethanol, 100 mM NaCl, 7 % MPD Resolution 3.41 Å R-free 0.294

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 Author chain B; PDBConstruct 1–460; UniProt 1–460

Selenoprotein S

Homo sapiens

UniProt Q9BQE4

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 49–122 Chain D; UniProt 49–122 Fragment:residues 49-122 Transitional endoplasmic reticulum ATPase × 2 (P55072) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;288 K;0.1 M Tris, pH 8, 15 % ethanol, 100 mM NaCl, 7 % MPD Resolution 3.41 Å R-free 0.294

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SELS_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 8–81; UniProt 49–122 Author chain D; PDBConstruct 8–81; UniProt 49–122

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 5kiw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5kiw
Deposition date deposition_date2016-06-17
Structure title titlep97 ND1-L198W in complex with VIMP
Keywords keywordsp97 adaptor protein, VCP-interacting membrane protein, VIMP, p97, HYDROLASE-MEMBRANE PROTEIN complex; HYDROLASE/MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier42.67
Radius of gyration Rg (electron density) rg_electron42.95
Forward intensity I(0) i0197274000.00
Molecular weight molecular_weight111890.0 kDa
Excluded volume excluded_volume139460 ų
Envelope volume envelope_volume221810 ų
Hydration-shell volume shell_volume44539 ų
Envelope diameter envelope_diameter168.8
Shell Rg shell_rg45.63
Envelope Rg envelope_rg43.04
Shape Rg shape_rg43.00
Total Rg total_rg42.96
Total atoms total_atoms7844
Residues n_residues987
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 dmax157.7
Rg (real space) rg_real42.92
Rg uncertainty (real space) rg_real_error1.83
I(0) (real space) i0_real1.9730e+08
I(0) uncertainty (real space) i0_real_error3.6610e+06
Rg (reciprocal space) rg_reciprocal42.68
I(0) (reciprocal space) i0_reciprocal197200000.0000
Solution quality estimate total_estimate0.8332
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary46.9
Skewness Skewness skewness0.470
Kurtosis Kurtosis kurtosis-0.116
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10270000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.704; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.863; Smooth: 0.852

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id5kiwB01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology330 — Vcp-like ATPase; Chain A, domain 2
Homologous superfamily homologous superfamily10
Domain ID domain_id5kiwB02
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_id5kiwB03
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)