2len

Solution structure of UCHL1 S18Y variant

Method: SOLUTION NMR Dmax: 59.5 Å Quality: GOOD

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

Ubiquitin carboxyl-terminal hydrolase isozyme L1

Homo sapiens

UniProt P09936

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 1–223 Mutation:S18Y No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Ionic strength (raw mmCIF value) 100;Pressure ambient NMR sample composition:0.7-0.8mM [U-99% 13C; U-99% 15N] UCHL1 S18Y variant-1, 20mM sodium phosphate-2, 100mM sodium chloride-3, 3mM DTT-4, 90% H2O-5, 10% D2O-6, 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.

13 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UCHL1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–223; UniProt 1–223

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 2len

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2len
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2len
Deposition date deposition_date2011-06-19
Structure title titleSolution structure of UCHL1 S18Y variant
Keywords keywordshydrolase; HYDROLASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier18.43
Radius of gyration Rg (electron density) rg_electron17.71
Forward intensity I(0) i03867550000.00
Molecular weight molecular_weight519130.0 kDa
Excluded volume excluded_volume645200 ų
Envelope volume envelope_volume70022 ų
Hydration-shell volume shell_volume26921 ų
Envelope diameter envelope_diameter68.3
Shell Rg shell_rg28.82
Envelope Rg envelope_rg21.14
Shape Rg shape_rg17.71
Total Rg total_rg17.86
Total atoms total_atoms65840
Residues n_residues4620
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 dmax59.5
Rg (real space) rg_real18.29
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real3.8680e+09
I(0) uncertainty (real space) i0_real_error5.0530e+07
Rg (reciprocal space) rg_reciprocal18.31
I(0) (reciprocal space) i0_reciprocal3868000000.0000
Solution quality estimate total_estimate0.7942
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary24.4
Skewness Skewness skewness0.077
Kurtosis Kurtosis kurtosis-0.387
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2890000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.778; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2lena1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.3 — Cysteine proteinases
Superfamily Superfamily superfamilyd.3.1 — Cysteine proteinases
Family Family familyd.3.1.6 — Ubiquitin carboxyl-terminal hydrolase UCH-L
Domain ID domain_idd2lena2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2lenA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology532 — Ubiquitin C-terminal Hydrolase UCH-l3
Homologous superfamily homologous superfamily10 — Peptidase C12, ubiquitin carboxyl-terminal hydrolase

8. Citations (1)

9. Files and Curves (10)