5jh5

Structural Basis for the Hierarchical Assembly of the Core of PRC1.1

Method: X-RAY DIFFRACTION Dmax: 115.8 Å Quality: GOOD

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

Lysine-specific demethylase 2B

Homo sapiens

UniProt Q8NHM5

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1059–1336 Fragment:RESIDUES 1059-1336 Non-standard monomer:Yes (specific site not provided by mmCIF) S-phase kinase-associated protein 1 × 1 (P63208) Polycomb group RING finger protein 1 × 1 (Q9BSM1) BCL-6 corepressor-like protein 1 × 1 (Q5H9F3) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.25;298 K;100 mM HEPES, 10 % 2-methyl-2,4-pentanediol, 10 mM NaCl Resolution 2.55 Å R-free 0.257

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 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KDM2B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–281; UniProt 1059–1336

S-phase kinase-associated protein 1

Homo sapiens

UniProt P63208

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 2–163 Fragment:Residues 2-163 Non-standard monomer:Yes (specific site not provided by mmCIF) Lysine-specific demethylase 2B × 1 (Q8NHM5) Polycomb group RING finger protein 1 × 1 (Q9BSM1) BCL-6 corepressor-like protein 1 × 1 (Q5H9F3) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.25;298 K;100 mM HEPES, 10 % 2-methyl-2,4-pentanediol, 10 mM NaCl Resolution 2.55 Å R-free 0.257

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.

71 other PDB entries and 97 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SKP1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–162; UniProt 2–163

Polycomb group RING finger protein 1

Homo sapiens

UniProt Q9BSM1

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 150–255 Fragment:RESIDUES 150-255 Non-standard monomer:Yes (specific site not provided by mmCIF) Lysine-specific demethylase 2B × 1 (Q8NHM5) S-phase kinase-associated protein 1 × 1 (P63208) BCL-6 corepressor-like protein 1 × 1 (Q5H9F3) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.25;298 K;100 mM HEPES, 10 % 2-methyl-2,4-pentanediol, 10 mM NaCl Resolution 2.55 Å R-free 0.257

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 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PCGF1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 4–109; UniProt 150–255

BCL-6 corepressor-like protein 1

Homo sapiens

UniProt Q5H9F3

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1594–1711 Fragment:RESIDUES 1594-1711 Non-standard monomer:Yes (specific site not provided by mmCIF) Lysine-specific demethylase 2B × 1 (Q8NHM5) S-phase kinase-associated protein 1 × 1 (P63208) Polycomb group RING finger protein 1 × 1 (Q9BSM1) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.25;298 K;100 mM HEPES, 10 % 2-methyl-2,4-pentanediol, 10 mM NaCl Resolution 2.55 Å R-free 0.257

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.

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

View Construct and Data Evidence
UniProt name BCORL_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 5–122; UniProt 1594–1711

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 5jh5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5jh5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5jh5
Deposition date deposition_date2016-04-20
Structure title titleStructural Basis for the Hierarchical Assembly of the Core of PRC1.1
Keywords keywordsgene repression, complex, transcription regulation, transcription repressor, METAL BINDING PROTEIN-TRANSCRIPTION complex; METAL BINDING PROTEIN/TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.95
Radius of gyration Rg (electron density) rg_electron30.82
Forward intensity I(0) i083050700.00
Molecular weight molecular_weight71348.0 kDa
Excluded volume excluded_volume88905 ų
Envelope volume envelope_volume115150 ų
Hydration-shell volume shell_volume32236 ų
Envelope diameter envelope_diameter119.4
Shell Rg shell_rg36.54
Envelope Rg envelope_rg30.72
Shape Rg shape_rg30.82
Total Rg total_rg31.34
Total atoms total_atoms4951
Residues n_residues594
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 dmax115.8
Rg (real space) rg_real31.03
Rg uncertainty (real space) rg_real_error1.37
I(0) (real space) i0_real8.3050e+07
I(0) uncertainty (real space) i0_real_error1.5510e+06
Rg (reciprocal space) rg_reciprocal31.00
I(0) (reciprocal space) i0_reciprocal83050000.0000
Solution quality estimate total_estimate0.8273
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.6
Skewness Skewness skewness0.400
Kurtosis Kurtosis kurtosis-0.197
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24440000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.681; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.716; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5jh5b1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.42 — POZ domain
Superfamily Superfamily superfamilyd.42.1 — POZ domain
Family Family familyd.42.1.0 — automated matches
Domain ID domain_idd5jh5b2
Class classa — All alpha proteins
Fold Fold folda.157 — Skp1 dimerisation domain-like
Superfamily Superfamily superfamilya.157.1 — Skp1 dimerisation domain-like
Family Family familya.157.1.1 — Skp1 dimerisation domain-like

CATH v4.4 (2 domains)

Domain ID domain_id5jh5B00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology710 — Potassium Channel Kv1.1; Chain A
Homologous superfamily homologous superfamily10 — Potassium Channel Kv1.1; Chain A
Domain ID domain_id5jh5C00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

8. Citations (1)

9. Files and Curves (10)