1q5w

Ubiquitin Recognition by Npl4 Zinc-Fingers

Method: SOLUTION NMR Dmax: 51.4 Å Quality: GOOD

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

homolog of yeast nuclear protein localization 4

Rattus norvegicus

UniProt Q9ES54

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 580–608 Fragment:Npl4 NZF domain (residues 580-608) Ubiquitin × 1 (P62988) ZN ZINC ION × 1 SOLUTION NMR NMR measurement conditions:pH 5.5;291 K;Ionic strength (raw mmCIF value) 70mM;Pressure ambient NMR measurement conditions:pH 5.5;291 K;Ionic strength (raw mmCIF value) 70mM;Pressure ambient NMR measurement conditions:pH 5.5;291 K;Ionic strength (raw mmCIF value) 70mM;Pressure ambient NMR measurement conditions:pH 5.5;291 K;Ionic strength (raw mmCIF value) 70mM;Pressure ambient NMR sample composition:1mM Npl4 NZF U-15N,13C; 2mM unlabeled-Ubiquitin; 20mM phosphate buffer pH 5.5, 50mM NaCl; 90% H2O, 10% | 90% H2O/10% D2O NMR sample composition:1mM Ubiquitin U-15N,13C; 2mM unlabeled-Npl4 NZF; 20mM phosphate buffer pH 5.5, 50mM NaCl; 90% H2O, 10% | 90% H2O/10% D2O NMR sample composition:1mM Ubiquitin U-15N; 2mM unlabeled-Npl4 NZF; 20mM phosphate buffer pH 5.5, 50mM | 90% H2O/10% D2O NMR sample composition:1mM Npl4 NZF U-15N; 2mM unlabeled-Ubiquitin; 20mM phosphate buffer pH 5.5, 50mM NaCl; 90% H2O, 10% | 90% H2O/10% D2O Resolution not provided

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NPL4_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–31; UniProt 580–608

Ubiquitin

Homo sapiens

UniProt P62988

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 B; UniProt 1–76 Not recorded homolog of yeast nuclear protein localization 4 × 1 (Q9ES54) ZN ZINC ION × 1 SOLUTION NMR NMR measurement conditions:pH 5.5;291 K;Ionic strength (raw mmCIF value) 70mM;Pressure ambient NMR measurement conditions:pH 5.5;291 K;Ionic strength (raw mmCIF value) 70mM;Pressure ambient NMR measurement conditions:pH 5.5;291 K;Ionic strength (raw mmCIF value) 70mM;Pressure ambient NMR measurement conditions:pH 5.5;291 K;Ionic strength (raw mmCIF value) 70mM;Pressure ambient NMR sample composition:1mM Npl4 NZF U-15N,13C; 2mM unlabeled-Ubiquitin; 20mM phosphate buffer pH 5.5, 50mM NaCl; 90% H2O, 10% | 90% H2O/10% D2O NMR sample composition:1mM Ubiquitin U-15N,13C; 2mM unlabeled-Npl4 NZF; 20mM phosphate buffer pH 5.5, 50mM NaCl; 90% H2O, 10% | 90% H2O/10% D2O NMR sample composition:1mM Ubiquitin U-15N; 2mM unlabeled-Npl4 NZF; 20mM phosphate buffer pH 5.5, 50mM | 90% H2O/10% D2O NMR sample composition:1mM Npl4 NZF U-15N; 2mM unlabeled-Ubiquitin; 20mM phosphate buffer pH 5.5, 50mM NaCl; 90% H2O, 10% | 90% H2O/10% D2O Resolution not provided

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.

83 other PDB entries and 138 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBIQ_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–76; UniProt 1–76

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 1q5w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1q5w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1q5w
Deposition date deposition_date2003-08-11
Structure title titleUbiquitin Recognition by Npl4 Zinc-Fingers
Keywords keywordsUbiquitin, Protein-Protein complex, Zinc-finger, Rubredoxin knuckle, NZF domain, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.14
Radius of gyration Rg (electron density) rg_electron13.74
Forward intensity I(0) i0871462000.00
Molecular weight molecular_weight240080.0 kDa
Excluded volume excluded_volume296620 ų
Envelope volume envelope_volume25095 ų
Hydration-shell volume shell_volume13712 ų
Envelope diameter envelope_diameter55.8
Shell Rg shell_rg21.40
Envelope Rg envelope_rg16.50
Shape Rg shape_rg13.75
Total Rg total_rg13.83
Total atoms total_atoms33420
Residues n_residues2140
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 dmax51.4
Rg (real space) rg_real14.12
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real8.7150e+08
I(0) uncertainty (real space) i0_real_error1.0300e+07
Rg (reciprocal space) rg_reciprocal14.12
I(0) (reciprocal space) i0_reciprocal871500000.0000
Solution quality estimate total_estimate0.8491
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.6
Skewness Skewness skewness0.278
Kurtosis Kurtosis kurtosis-0.221
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha194400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.708; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.915; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1q5wa1
Class classg — Small proteins
Fold Fold foldg.41 — Rubredoxin-like
Superfamily Superfamily superfamilyg.41.11 — Ran binding protein zinc finger-like
Family Family familyg.41.11.1 — Ran binding protein zinc finger-like
Domain ID domain_idd1q5wa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1q5wb_
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.15.1.1 — Ubiquitin-related

CATH v4.4 (1 domains)

Domain ID domain_id1q5wB00
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 (2)

9. Files and Curves (10)