5bo0

Crystal structure of Human MCM2 HBD and ASF1b chaperoning a histone H3.2-H4 dimer

Method: X-RAY DIFFRACTION Dmax: 85.6 Å Quality: GOOD

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

Histone H3.2

Homo sapiens

UniProt Q71DI3

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 57–136 Fragment:UNP residues 57-136 Histone H4 × 1 (P62805) DNA replication licensing factor MCM2 × 1 (P49736) Histone chaperone ASF1B × 1 (Q9NVP2) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;3.2 M sodium formate, 0.1 M Tris, pH 8.5 Resolution 2.91 Å R-free 0.238

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.

139 other PDB entries and 157 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H32_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–80; UniProt 57–136

Histone H4

Homo sapiens

UniProt P62805

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 2–103 Not recorded Histone H3.2 × 1 (Q71DI3) DNA replication licensing factor MCM2 × 1 (P49736) Histone chaperone ASF1B × 1 (Q9NVP2) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;3.2 M sodium formate, 0.1 M Tris, pH 8.5 Resolution 2.91 Å R-free 0.238

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.

581 other PDB entries and 633 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–102; UniProt 2–103

DNA replication licensing factor MCM2

Homo sapiens

UniProt P49736

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 61–130 Fragment:UNP residues 61-130 Histone H3.2 × 1 (Q71DI3) Histone H4 × 1 (P62805) Histone chaperone ASF1B × 1 (Q9NVP2) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;3.2 M sodium formate, 0.1 M Tris, pH 8.5 Resolution 2.91 Å R-free 0.238

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.

38 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MCM2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–70; UniProt 61–130

Histone chaperone ASF1B

Homo sapiens

UniProt Q9NVP2

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 1–158 Fragment:UNP residues 1-158 Histone H3.2 × 1 (Q71DI3) Histone H4 × 1 (P62805) DNA replication licensing factor MCM2 × 1 (P49736) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;3.2 M sodium formate, 0.1 M Tris, pH 8.5 Resolution 2.91 Å R-free 0.238

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.

3 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ASF1B_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–158; UniProt 1–158

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 5bo0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5bo0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5bo0
Deposition date deposition_date2015-05-26
Structure title titleCrystal structure of Human MCM2 HBD and ASF1b chaperoning a histone H3.2-H4 dimer
Keywords keywordsDNA replication, MCM2, ASF1b, H3.2-H4 dimer, CHAPERONE-DNA BINDING PROTEIN complex; CHAPERONE/DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.35
Radius of gyration Rg (electron density) rg_electron23.31
Forward intensity I(0) i030812200.00
Molecular weight molecular_weight42159.0 kDa
Excluded volume excluded_volume52724 ų
Envelope volume envelope_volume65971 ų
Hydration-shell volume shell_volume23886 ų
Envelope diameter envelope_diameter88.9
Shell Rg shell_rg29.72
Envelope Rg envelope_rg23.84
Shape Rg shape_rg23.30
Total Rg total_rg24.16
Total atoms total_atoms2970
Residues n_residues374
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 dmax85.6
Rg (real space) rg_real24.33
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real3.0810e+07
I(0) uncertainty (real space) i0_real_error5.0230e+05
Rg (reciprocal space) rg_reciprocal24.34
I(0) (reciprocal space) i0_reciprocal30810000.0000
Solution quality estimate total_estimate0.8627
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.9
Skewness Skewness skewness0.320
Kurtosis Kurtosis kurtosis-0.290
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9839000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.780; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.904; Smooth: 0.974

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd5bo0a_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones
Domain ID domain_idd5bo0b_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones
Domain ID domain_idd5bo0d_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.22 — ASF1-like
Family Family familyb.1.22.1 — ASF1-like

CATH v4.4 (3 domains)

Domain ID domain_id5bo0A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id5bo0B00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id5bo0D00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1490 — Histone chaperone ASF1-like

8. Citations (1)

9. Files and Curves (10)