2mur

Solution Structure of the Human FAAP20 UBZ-Ubiquitin Complex

Method: SOLUTION NMR Dmax: 52.0 Å Quality: GOOD

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

Fanconi anemia-associated protein of 20 kDa

Homo sapiens

UniProt Q6NZ36

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 140–180 Fragment:UBZ, UNP residues 140-180 Ubiquitin × 1 (P62987) ZN ZINC ION × 1 SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 100;Pressure ambient NMR sample composition:1 mM [U-100% 13C; U-100% 15N] Ubiquitin, 25 mM sodium phosphate, 100 mM potassium chloride, 2 mM UBZ, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.8 mM [U-100% 13C; U-100% 15N] UBZ, 0.8 mM [U-100% 13C; U-100% 15N] Ubiquitin, 25 mM sodium phosphate, 100 mM potassium chloride, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:3 mM [U-100% 13C; U-100% 15N] Ubiquitin, 25 mM sodium phosphate, 100 mM potassium chloride, 3 mM [U-100% 13C; U-100% 15N] UBZ, 100% D2O | 100% D2O NMR sample composition:3 mM Ubiquitin, 25 mM sodium phosphate, 100 mM potassium chloride, 3 mM [U-100% 13C; U-100% 15N] UBZ, 100% D2O | 100% D2O NMR sample composition:3 mM [U-100% 13C; U-100% 15N] Ubiquitin, 25 mM sodium phosphate, 100 mM potassium chloride, 3 mM UBZ, 100% D2O | 100% D2O NMR sample composition:1 mM [U-100% 13C; U-100% 15N] Ubiquitin, 25 mM sodium phosphate, 100 mM potassium chloride, 2 mM UBZ, 100% D2O | 100% D2O NMR sample composition:0.8 mM [U-100% 13C; U-100% 15N] UBZ, 0.8 mM [U-100% 13C; U-100% 15N] Ubiquitin, 25 mM sodium phosphate, 100 mM potassium chloride, 100% D2O | 100% 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.

2 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FAP20_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–44; UniProt 140–180

Ubiquitin

Homo sapiens

UniProt P62987

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 Fanconi anemia-associated protein of 20 kDa × 1 (Q6NZ36) ZN ZINC ION × 1 SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 100;Pressure ambient NMR sample composition:1 mM [U-100% 13C; U-100% 15N] Ubiquitin, 25 mM sodium phosphate, 100 mM potassium chloride, 2 mM UBZ, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.8 mM [U-100% 13C; U-100% 15N] UBZ, 0.8 mM [U-100% 13C; U-100% 15N] Ubiquitin, 25 mM sodium phosphate, 100 mM potassium chloride, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:3 mM [U-100% 13C; U-100% 15N] Ubiquitin, 25 mM sodium phosphate, 100 mM potassium chloride, 3 mM [U-100% 13C; U-100% 15N] UBZ, 100% D2O | 100% D2O NMR sample composition:3 mM Ubiquitin, 25 mM sodium phosphate, 100 mM potassium chloride, 3 mM [U-100% 13C; U-100% 15N] UBZ, 100% D2O | 100% D2O NMR sample composition:3 mM [U-100% 13C; U-100% 15N] Ubiquitin, 25 mM sodium phosphate, 100 mM potassium chloride, 3 mM UBZ, 100% D2O | 100% D2O NMR sample composition:1 mM [U-100% 13C; U-100% 15N] Ubiquitin, 25 mM sodium phosphate, 100 mM potassium chloride, 2 mM UBZ, 100% D2O | 100% D2O NMR sample composition:0.8 mM [U-100% 13C; U-100% 15N] UBZ, 0.8 mM [U-100% 13C; U-100% 15N] Ubiquitin, 25 mM sodium phosphate, 100 mM potassium chloride, 100% D2O | 100% 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.

153 other PDB entries and 174 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL40_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–78; 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 2mur

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2mur
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2mur
Deposition date deposition_date2014-09-16
Structure title titleSolution Structure of the Human FAAP20 UBZ-Ubiquitin Complex
Keywords keywordsUBZ, FAAP20, zinc-finger, Fanconi Anemia, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.89
Radius of gyration Rg (electron density) rg_electron14.25
Forward intensity I(0) i0280632000.00
Molecular weight molecular_weight136660.0 kDa
Excluded volume excluded_volume169600 ų
Envelope volume envelope_volume26383 ų
Hydration-shell volume shell_volume14250 ų
Envelope diameter envelope_diameter54.4
Shell Rg shell_rg21.57
Envelope Rg envelope_rg16.40
Shape Rg shape_rg14.23
Total Rg total_rg14.55
Total atoms total_atoms19090
Residues n_residues1220
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 dmax52.0
Rg (real space) rg_real14.84
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real2.8060e+08
I(0) uncertainty (real space) i0_real_error3.4780e+06
Rg (reciprocal space) rg_reciprocal14.84
I(0) (reciprocal space) i0_reciprocal280600000.0000
Solution quality estimate total_estimate0.7745
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary18.4
Skewness Skewness skewness0.229
Kurtosis Kurtosis kurtosis-0.274
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha387800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.700; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.975; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2murb1
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
Domain ID domain_idd2murb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

8. Citations (1)

9. Files and Curves (10)