6fdk

Structure of Chlamydia trachomatis effector protein Cdu1 bound to ubiquitin

Method: X-RAY DIFFRACTION Dmax: 67.9 Å Quality: EXCELLENT

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

Deubiquitinase and deneddylase Dub1

Chlamydia trachomatis 434/Bu

UniProt B0B9A0

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 155–401 Mutation:C174A, C226S, C386A Polyubiquitin-B × 1 (P0CG47) CL CHLORIDE ION × 1 AYE prop-2-en-1-amine × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;0.1 M MES pH 6.5, 12% PEG 20000 Resolution 1.60 Å R-free 0.203

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.

5 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDUB1_CHLT2
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 20–266; UniProt 155–401

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 B; UniProt 1–75 Not recorded Deubiquitinase and deneddylase Dub1 × 1 (B0B9A0) CL CHLORIDE ION × 1 AYE prop-2-en-1-amine × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;0.1 M MES pH 6.5, 12% PEG 20000 Resolution 1.60 Å R-free 0.203

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 B; PDBConstruct 1–75; UniProt 1–75

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 6fdk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6fdk
Deposition date deposition_date2017-12-25
Structure title titleStructure of Chlamydia trachomatis effector protein Cdu1 bound to ubiquitin
Keywords keywordsChlaDUB1, CE protease, DUB, Ubiquitin., HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.75
Radius of gyration Rg (electron density) rg_electron20.38
Forward intensity I(0) i020880500.00
Molecular weight molecular_weight36160.0 kDa
Excluded volume excluded_volume45911 ų
Envelope volume envelope_volume54323 ų
Hydration-shell volume shell_volume22302 ų
Envelope diameter envelope_diameter69.0
Shell Rg shell_rg27.09
Envelope Rg envelope_rg20.58
Shape Rg shape_rg20.36
Total Rg total_rg21.36
Total atoms total_atoms2548
Residues n_residues317
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 dmax67.9
Rg (real space) rg_real21.65
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real2.0880e+07
I(0) uncertainty (real space) i0_real_error2.6100e+05
Rg (reciprocal space) rg_reciprocal21.67
I(0) (reciprocal space) i0_reciprocal20880000.0000
Solution quality estimate total_estimate0.9025
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.4
Skewness Skewness skewness0.236
Kurtosis Kurtosis kurtosis-0.353
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5141000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.911; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd6fdkb_
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

8. Citations (1)

9. Files and Curves (10)