2kvr

Solution NMR structure of human ubiquitin specific protease Usp7 UBL domain (residues 537-664). NESG target hr4395c/ SGC-Toronto

Method: SOLUTION NMR Dmax: 57.8 Å Quality: GOOD

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

Ubiquitin carboxyl-terminal hydrolase 7

Homo sapiens

UniProt Q93009

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 537–664 Fragment:ubiquitin-like domain (residues 537-664) No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 250;Pressure ambient NMR sample composition:0.8-1.2 mM [U-100% 13C; U-100% 15N] protein, 20 mM sodium phosphate, pH 7.0, 250 mM sodium chloride, 2 mM DTT, 0.5 mM PMSF, 1 mM benzamidine, 1 mM TCEP, 90% H2O/10% D2O | 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.

84 other PDB entries and 145 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBP7_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–130; UniProt 537–664

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 2kvr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2kvr
Deposition date deposition_date2010-03-25
Structure title titleSolution NMR structure of human ubiquitin specific protease Usp7 UBL domain (residues 537-664). NESG target hr4395c/ SGC-Toronto
Keywords keywords;usp7, ubiquitin-like domain, UBL, ubiquitin specific protease, Host-virus interaction, Hydrolase, Nucleus, Protease, Thiol protease, Structural Genomics, PSI-2, Protein Structure Initiative, Northeast Structural Genomics Consortium, NESG, SGC, protein binding ;; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier16.54
Radius of gyration Rg (electron density) rg_electron15.96
Forward intensity I(0) i01360670000.00
Molecular weight molecular_weight300340.0 kDa
Excluded volume excluded_volume370650 ų
Envelope volume envelope_volume38416 ų
Hydration-shell volume shell_volume17678 ų
Envelope diameter envelope_diameter62.2
Shell Rg shell_rg24.47
Envelope Rg envelope_rg18.98
Shape Rg shape_rg15.94
Total Rg total_rg16.14
Total atoms total_atoms41580
Residues n_residues2560
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 dmax57.8
Rg (real space) rg_real16.53
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real1.3610e+09
I(0) uncertainty (real space) i0_real_error1.5690e+07
Rg (reciprocal space) rg_reciprocal16.53
I(0) (reciprocal space) i0_reciprocal1361000000.0000
Solution quality estimate total_estimate0.8696
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.8
Skewness Skewness skewness0.336
Kurtosis Kurtosis kurtosis-0.218
Angular range angular_range— – 0.4800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha464600.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.779; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.965; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (2)

9. Files and Curves (10)