5k1c

Crystal structure of the UAF1/WDR20/USP12 complex

Method: X-RAY DIFFRACTION Dmax: 135.2 Å Quality: GOOD

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

Ubiquitin carboxyl-terminal hydrolase 12

Homo sapiens

UniProt O75317

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 16–370 Fragment:residues 16-370 WD repeat-containing protein 48 × 1 (Q8TAF3) WD repeat-containing protein 20 × 1 (Q8TBZ3) ZN ZINC ION × 1 PO4 PHOSPHATE ION × 1 TAM TRIS(HYDROXYETHYL)AMINOMETHANE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;277 K;0.1 M MES, 1.3 M ammonium phosphate dibasic Resolution 3.00 Å R-free 0.271

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.

4 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBP12_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–355; UniProt 16–370

WD repeat-containing protein 48

Homo sapiens

UniProt Q8TAF3

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–563 Fragment:residues 1-563 Ubiquitin carboxyl-terminal hydrolase 12 × 1 (O75317) WD repeat-containing protein 20 × 1 (Q8TBZ3) ZN ZINC ION × 1 PO4 PHOSPHATE ION × 1 TAM TRIS(HYDROXYETHYL)AMINOMETHANE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;277 K;0.1 M MES, 1.3 M ammonium phosphate dibasic Resolution 3.00 Å R-free 0.271

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.

18 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WDR48_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–563; UniProt 1–563

WD repeat-containing protein 20

Homo sapiens

UniProt Q8TBZ3

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–569 Not recorded Ubiquitin carboxyl-terminal hydrolase 12 × 1 (O75317) WD repeat-containing protein 48 × 1 (Q8TAF3) ZN ZINC ION × 1 PO4 PHOSPHATE ION × 1 TAM TRIS(HYDROXYETHYL)AMINOMETHANE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;277 K;0.1 M MES, 1.3 M ammonium phosphate dibasic Resolution 3.00 Å R-free 0.271

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.

2 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WDR20_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–569; UniProt 1–569

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 5k1c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5k1c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5k1c
Deposition date deposition_date2016-05-18
Structure title titleCrystal structure of the UAF1/WDR20/USP12 complex
Keywords keywords;WD40 repeat domain, WDR20, USP12, UAF1, WDR48, deubiquitinating enzyme, Ubiquitin-specific protease, USP1-associated factor 1, HYDROLASE ;; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.59
Radius of gyration Rg (electron density) rg_electron37.26
Forward intensity I(0) i0284754000.00
Molecular weight molecular_weight135800.0 kDa
Excluded volume excluded_volume169330 ų
Envelope volume envelope_volume225760 ų
Hydration-shell volume shell_volume50354 ų
Envelope diameter envelope_diameter139.8
Shell Rg shell_rg43.37
Envelope Rg envelope_rg37.02
Shape Rg shape_rg37.29
Total Rg total_rg37.51
Total atoms total_atoms9558
Residues n_residues1224
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 dmax135.2
Rg (real space) rg_real37.64
Rg uncertainty (real space) rg_real_error1.37
I(0) (real space) i0_real2.8480e+08
I(0) uncertainty (real space) i0_real_error5.4450e+06
Rg (reciprocal space) rg_reciprocal37.61
I(0) (reciprocal space) i0_reciprocal284700000.0000
Solution quality estimate total_estimate0.8612
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary38.6
Skewness Skewness skewness0.339
Kurtosis Kurtosis kurtosis-0.413
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha113600000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.748; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.956; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5k1ca_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.3 — Cysteine proteinases
Superfamily Superfamily superfamilyd.3.1 — Cysteine proteinases
Family Family familyd.3.1.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id5k1cC00
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase

8. Citations (1)

9. Files and Curves (10)