2le8

The protein complex for DNA replication

Method: SOLUTION NMR Dmax: 73.2 Å Quality: REASONABLE

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

DNA replication licensing factor MCM6

Homo sapiens

UniProt Q14566

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 708–821 Fragment:UNP residues 708-821 Mutation:C18S DNA replication factor Cdt1 × 1 (Q9H211) SOLUTION NMR NMR measurement conditions:pH 6.5;310 K;Ionic strength (raw mmCIF value) 3;Pressure ambient NMR sample composition:25 mM MES-1, 300 mM sodium chloride-2, 1 % glycerol-3, 0.8 mM [U-100% 13C; U-100% 15N] entity_2-4, 1 mM entity_1-5, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:25 mM [U-100% 15N] MES-6, 300 mM sodium chloride-7, 1 % glycerol-8, 0.8 mM [U-100% 13C; U-100% 15N] entity_1-9, 1.0 mM entity_2-10, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:25 mM MES-11, 300 mM sodium chloride-12, 1 % glycerol-13, 0.8 mM [U-100% 13C; U-100% 15N] entity_1-14, 1.0 mM entity_2-15, 100% D2O | 100% D2O NMR sample composition:25 mM MES-16, 300 mM sodium chloride-17, 1 % glycerol-18, 0.8 mM [U-100% 13C; U-100% 15N] entity_2-19, 1.0 mM entity_1-20, 100% D2O | 100% D2O Resolution not provided

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.

29 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MCM6_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–114; UniProt 708–821

DNA replication factor Cdt1

Homo sapiens

UniProt Q9H211

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 413–440 Fragment:UNP residues 413-440 DNA replication licensing factor MCM6 × 1 (Q14566) SOLUTION NMR NMR measurement conditions:pH 6.5;310 K;Ionic strength (raw mmCIF value) 3;Pressure ambient NMR sample composition:25 mM MES-1, 300 mM sodium chloride-2, 1 % glycerol-3, 0.8 mM [U-100% 13C; U-100% 15N] entity_2-4, 1 mM entity_1-5, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:25 mM [U-100% 15N] MES-6, 300 mM sodium chloride-7, 1 % glycerol-8, 0.8 mM [U-100% 13C; U-100% 15N] entity_1-9, 1.0 mM entity_2-10, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:25 mM MES-11, 300 mM sodium chloride-12, 1 % glycerol-13, 0.8 mM [U-100% 13C; U-100% 15N] entity_1-14, 1.0 mM entity_2-15, 100% D2O | 100% D2O NMR sample composition:25 mM MES-16, 300 mM sodium chloride-17, 1 % glycerol-18, 0.8 mM [U-100% 13C; U-100% 15N] entity_2-19, 1.0 mM entity_1-20, 100% D2O | 100% D2O Resolution not provided

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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDT1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–28; UniProt 413–440

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 2le8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2le8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2le8
Deposition date deposition_date2011-06-14
Structure title titleThe protein complex for DNA replication
Keywords keywordsDNA replication, REPLICATION; REPLICATION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier18.48
Radius of gyration Rg (electron density) rg_electron17.83
Forward intensity I(0) i01386960000.00
Molecular weight molecular_weight316040.0 kDa
Excluded volume excluded_volume396450 ų
Envelope volume envelope_volume68596 ų
Hydration-shell volume shell_volume25108 ų
Envelope diameter envelope_diameter84.3
Shell Rg shell_rg30.10
Envelope Rg envelope_rg23.75
Shape Rg shape_rg17.82
Total Rg total_rg18.15
Total atoms total_atoms44802
Residues n_residues2717
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 dmax73.2
Rg (real space) rg_real18.54
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real1.3870e+09
I(0) uncertainty (real space) i0_real_error1.8690e+07
Rg (reciprocal space) rg_reciprocal18.53
I(0) (reciprocal space) i0_reciprocal1387000000.0000
Solution quality estimate total_estimate0.6973
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary19.1
Skewness Skewness skewness0.474
Kurtosis Kurtosis kurtosis0.021
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1222000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.478; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.627; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2le8A00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily870

8. Citations (1)

9. Files and Curves (10)