5kyc

Crystal structure of USP7 catalytic domain [V302K] mutant in complex with ubiquitin (malonate bound)

Method: X-RAY DIFFRACTION Dmax: 78.3 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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 192–538 Fragment:UNP residues 192-538 Mutation:V302K Polyubiquitin-B × 1 (P0CG47) MLA MALONIC ACID × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4;292 K;8% tacsimate pH 4.0, 20% PEG3350 Resolution 1.43 Å R-free 0.192

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 Q93009-3
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 5–351; UniProt 192–538

Polyubiquitin-B

Homo sapiens

UniProt P0CG47

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 C; UniProt 1–76 Fragment:UNP residues 1-76 Ubiquitin carboxyl-terminal hydrolase 7 × 1 (Q93009) MLA MALONIC ACID × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4;292 K;8% tacsimate pH 4.0, 20% PEG3350 Resolution 1.43 Å R-free 0.192

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.

278 other PDB entries and 429 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBB_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; 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 5kyc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5kyc
Deposition date deposition_date2016-07-21
Structure title titleCrystal structure of USP7 catalytic domain [V302K] mutant in complex with ubiquitin (malonate bound)
Keywords keywordsUSP7 catalytic domain, deubiquitinase, V302K mutation, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.37
Radius of gyration Rg (electron density) rg_electron21.97
Forward intensity I(0) i039614800.00
Molecular weight molecular_weight48112.0 kDa
Excluded volume excluded_volume60050 ų
Envelope volume envelope_volume70858 ų
Hydration-shell volume shell_volume26533 ų
Envelope diameter envelope_diameter80.4
Shell Rg shell_rg29.35
Envelope Rg envelope_rg22.20
Shape Rg shape_rg21.96
Total Rg total_rg22.88
Total atoms total_atoms3383
Residues n_residues416
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 dmax78.3
Rg (real space) rg_real23.26
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real3.9610e+07
I(0) uncertainty (real space) i0_real_error5.5630e+05
Rg (reciprocal space) rg_reciprocal23.29
I(0) (reciprocal space) i0_reciprocal39620000.0000
Solution quality estimate total_estimate0.8802
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary28.9
Skewness Skewness skewness0.221
Kurtosis Kurtosis kurtosis-0.332
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7133000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.813; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5kycb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.3 — Cysteine proteinases
Superfamily Superfamily superfamilyd.3.1 — Cysteine proteinases
Family Family familyd.3.1.9 — Ubiquitin carboxyl-terminal hydrolase, UCH
Domain ID domain_idd5kycc_
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_id5kycB02
Class class2 — Mainly Beta
Architecture architecture20 — Single Sheet
Topology topology210 — ubp-family deubiquitinating enzyme fold
Homologous superfamily homologous superfamily10 — ubp-family deubiquitinating enzyme superfamily

8. Citations (1)

9. Files and Curves (10)