6iim

USP14 catalytic domain with IU1-206

Method: X-RAY DIFFRACTION Dmax: 113.6 Å Quality: GOOD

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

Ubiquitin carboxyl-terminal hydrolase 14

Homo sapiens

UniProt P54578

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 96–494 Chain B; UniProt 96–494 Fragment:catalytic domain A8L 1-[1-(4-chlorophenyl)-2,5-dimethyl-1H-pyrrol-3-yl]-2-(4-hydroxypiperidin-1-yl)ethan-1-one × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;PEG 3350, NH4F, Cscl, glycine Resolution 2.21 Å R-free 0.247

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.

22 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBP14_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–399; UniProt 96–494 Author chain B; PDBConstruct 1–399; UniProt 96–494

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 6iim

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6iim
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6iim
Deposition date deposition_date2018-10-07
Structure title titleUSP14 catalytic domain with IU1-206
Keywords keywordsUSP14 inhibitor complex, STRUCTURAL PROTEIN, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.90
Radius of gyration Rg (electron density) rg_electron33.69
Forward intensity I(0) i091927300.00
Molecular weight molecular_weight77472.0 kDa
Excluded volume excluded_volume97466 ų
Envelope volume envelope_volume128330 ų
Hydration-shell volume shell_volume33461 ų
Envelope diameter envelope_diameter122.3
Shell Rg shell_rg37.82
Envelope Rg envelope_rg34.10
Shape Rg shape_rg33.69
Total Rg total_rg34.06
Total atoms total_atoms5438
Residues n_residues669
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 dmax113.6
Rg (real space) rg_real34.16
Rg uncertainty (real space) rg_real_error1.07
I(0) (real space) i0_real9.1930e+07
I(0) uncertainty (real space) i0_real_error1.4500e+06
Rg (reciprocal space) rg_reciprocal34.00
I(0) (reciprocal space) i0_reciprocal91910000.0000
Solution quality estimate total_estimate0.8218
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.4
Skewness Skewness skewness0.508
Kurtosis Kurtosis kurtosis-0.441
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13110000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.769; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.706; Smooth: 0.665

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd6iima_
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_idd6iimb_
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

CATH v4.4 (2 domains)

Domain ID domain_id6iimA00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology70 — Cathepsin B; Chain A
Homologous superfamily homologous superfamily10 — Cysteine proteinases
Domain ID domain_id6iimB00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology70 — Cathepsin B; Chain A
Homologous superfamily homologous superfamily10 — Cysteine proteinases

8. Citations (1)

9. Files and Curves (10)