4ocl

Crystal Structure of the Rpn8-Rpn11 MPN domain heterodimer, crystal form Ia

Method: X-RAY DIFFRACTION Dmax: 140.2 Å Quality: GOOD

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

26S proteasome regulatory subunit RPN8

Saccharomyces cerevisiae

UniProt Q08723

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 1–176 Fragment:UNP residues 1-176 26S proteasome regulatory subunit RPN11 × 1 (P43588) Nb1 × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROPS;pH 6;291 K;50 mM MES, pH 6.0, 200 mM calcium acetate, 22% PEG3350, VAPOR DIFFUSION, SITTING DROPS, temperature 291K Resolution 2.40 Å R-free 0.252
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 1–176 Fragment:UNP residues 1-176 26S proteasome regulatory subunit RPN11 × 1 (P43588) Nb1 × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROPS;pH 6;291 K;50 mM MES, pH 6.0, 200 mM calcium acetate, 22% PEG3350, VAPOR DIFFUSION, SITTING DROPS, temperature 291K Resolution 2.40 Å R-free 0.252

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.

37 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPN8_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–178; UniProt 1–176 Author chain D; PDBConstruct 3–178; UniProt 1–176

26S proteasome regulatory subunit RPN11

Saccharomyces cerevisiae

UniProt P43588

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 1–220 Fragment:UNP residues 1-220 26S proteasome regulatory subunit RPN8 × 1 (Q08723) Nb1 × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROPS;pH 6;291 K;50 mM MES, pH 6.0, 200 mM calcium acetate, 22% PEG3350, VAPOR DIFFUSION, SITTING DROPS, temperature 291K Resolution 2.40 Å R-free 0.252
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 1–220 Fragment:UNP residues 1-220 26S proteasome regulatory subunit RPN8 × 1 (Q08723) Nb1 × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROPS;pH 6;291 K;50 mM MES, pH 6.0, 200 mM calcium acetate, 22% PEG3350, VAPOR DIFFUSION, SITTING DROPS, temperature 291K Resolution 2.40 Å R-free 0.252

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.

37 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPN11_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–220; UniProt 1–220 Author chain E; PDBConstruct 1–220; UniProt 1–220

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 4ocl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ocl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4ocl
Deposition date deposition_date2014-01-09
Structure title titleCrystal Structure of the Rpn8-Rpn11 MPN domain heterodimer, crystal form Ia
Keywords keywords26S proteasome, isopeptidase activity, regulatory particle, lid, ubiquitin, HYDROLASE, PROTEIN BINDING; HYDROLASE, PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.03
Radius of gyration Rg (electron density) rg_electron36.63
Forward intensity I(0) i0165278000.00
Molecular weight molecular_weight103330.0 kDa
Excluded volume excluded_volume129270 ų
Envelope volume envelope_volume172950 ų
Hydration-shell volume shell_volume40657 ų
Envelope diameter envelope_diameter148.5
Shell Rg shell_rg40.95
Envelope Rg envelope_rg36.65
Shape Rg shape_rg36.68
Total Rg total_rg36.75
Total atoms total_atoms7265
Residues n_residues942
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 dmax140.2
Rg (real space) rg_real37.30
Rg uncertainty (real space) rg_real_error1.46
I(0) (real space) i0_real1.6530e+08
I(0) uncertainty (real space) i0_real_error3.0840e+06
Rg (reciprocal space) rg_reciprocal37.14
I(0) (reciprocal space) i0_reciprocal165300000.0000
Solution quality estimate total_estimate0.8098
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.1
Skewness Skewness skewness0.501
Kurtosis Kurtosis kurtosis-0.163
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24340000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.652; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.595; Smooth: 0.972

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (10 domains)

Domain ID domain_idd4ocla_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.97 — Cytidine deaminase-like
Superfamily Superfamily superfamilyc.97.3 — JAB1/MPN domain
Family Family familyc.97.3.1 — JAB1/MPN domain
Domain ID domain_idd4oclb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.97 — Cytidine deaminase-like
Superfamily Superfamily superfamilyc.97.3 — JAB1/MPN domain
Family Family familyc.97.3.1 — JAB1/MPN domain
Domain ID domain_idd4oclc1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd4oclc2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4oclc3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4ocld_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.97 — Cytidine deaminase-like
Superfamily Superfamily superfamilyc.97.3 — JAB1/MPN domain
Family Family familyc.97.3.1 — JAB1/MPN domain
Domain ID domain_idd4ocle_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.97 — Cytidine deaminase-like
Superfamily Superfamily superfamilyc.97.3 — JAB1/MPN domain
Family Family familyc.97.3.1 — JAB1/MPN domain
Domain ID domain_idd4oclf1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd4oclf2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4oclf3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (6 domains)

Domain ID domain_id4oclA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology140 — Cytidine Deaminase; domain 2
Homologous superfamily homologous superfamily10 — Cytidine Deaminase, domain 2
Domain ID domain_id4oclB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology140 — Cytidine Deaminase; domain 2
Homologous superfamily homologous superfamily10 — Cytidine Deaminase, domain 2
Domain ID domain_id4oclC00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4oclD00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology140 — Cytidine Deaminase; domain 2
Homologous superfamily homologous superfamily10 — Cytidine Deaminase, domain 2
Domain ID domain_id4oclE00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology140 — Cytidine Deaminase; domain 2
Homologous superfamily homologous superfamily10 — Cytidine Deaminase, domain 2
Domain ID domain_id4oclF00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)