2lp0

The solution structure of homeodomain-protein complex

Method: SOLUTION NMR Dmax: 51.1 Å Quality: GOOD

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

Homeobox protein Hox-C9

Homo sapiens

UniProt P31274

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 192–251 Fragment:UNP residues 192-251 Geminin × 1 (O75496) SOLUTION NMR NMR measurement conditions:pH 6.5;296 K;Ionic strength (raw mmCIF value) 0.125;Pressure ambient NMR sample composition:0.8 mM [U-100% 13C; U-100% 15N] Hox-C9-1, 1.0 mM Geminin-2, 25 mM potassium phosphate-3, 100 mM sodium chloride-4, 5 mM DTT-5, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1.0 mM Hox-C9-6, 0.8 mM [U-100% 13C; U-100% 15N] Geminin-7, 25 mM potassium phosphate-8, 100 mM sodium chloride-9, 5 mM DTT-10, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.8 mM [U-100% 13C; U-100% 15N] Hox-C9-11, 1.0 mM Geminin-12, 25 mM potassium phosphate-13, 100 mM sodium chloride-14, 5 mM DTT-15, 100% D2O | 100% D2O NMR sample composition:1.0 mM Hox-C9-16, 0.8 mM [U-100% 13C; U-100% 15N] Geminin-17, 25 mM potassium phosphate-18, 100 mM sodium chloride-19, 5 mM DTT-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.

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

View Construct and Data Evidence
UniProt name HXC9_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–60; UniProt 192–251

Geminin

Homo sapiens

UniProt O75496

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 171–190 Fragment:UNP residues 171-190 Homeobox protein Hox-C9 × 1 (P31274) SOLUTION NMR NMR measurement conditions:pH 6.5;296 K;Ionic strength (raw mmCIF value) 0.125;Pressure ambient NMR sample composition:0.8 mM [U-100% 13C; U-100% 15N] Hox-C9-1, 1.0 mM Geminin-2, 25 mM potassium phosphate-3, 100 mM sodium chloride-4, 5 mM DTT-5, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1.0 mM Hox-C9-6, 0.8 mM [U-100% 13C; U-100% 15N] Geminin-7, 25 mM potassium phosphate-8, 100 mM sodium chloride-9, 5 mM DTT-10, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.8 mM [U-100% 13C; U-100% 15N] Hox-C9-11, 1.0 mM Geminin-12, 25 mM potassium phosphate-13, 100 mM sodium chloride-14, 5 mM DTT-15, 100% D2O | 100% D2O NMR sample composition:1.0 mM Hox-C9-16, 0.8 mM [U-100% 13C; U-100% 15N] Geminin-17, 25 mM potassium phosphate-18, 100 mM sodium chloride-19, 5 mM DTT-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 GEMI_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–20; UniProt 171–190

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 2lp0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2lp0
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2lp0
Deposition date deposition_date2012-01-29
Structure title titleThe solution structure of homeodomain-protein complex
Keywords keywordshomeodomain, TRANSCRIPTION-CELL CYCLE complex; TRANSCRIPTION/CELL CYCLE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.04
Radius of gyration Rg (electron density) rg_electron13.51
Forward intensity I(0) i0156790000.00
Molecular weight molecular_weight100530.0 kDa
Excluded volume excluded_volume124600 ų
Envelope volume envelope_volume32661 ų
Hydration-shell volume shell_volume16264 ų
Envelope diameter envelope_diameter56.5
Shell Rg shell_rg23.21
Envelope Rg envelope_rg17.54
Shape Rg shape_rg13.50
Total Rg total_rg14.01
Total atoms total_atoms14040
Residues n_residues800
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 dmax51.1
Rg (real space) rg_real14.05
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real1.5680e+08
I(0) uncertainty (real space) i0_real_error1.6730e+06
Rg (reciprocal space) rg_reciprocal14.05
I(0) (reciprocal space) i0_reciprocal156800000.0000
Solution quality estimate total_estimate0.8359
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.2
Skewness Skewness skewness0.393
Kurtosis Kurtosis kurtosis-0.018
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha314400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.655; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.907; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2lp0a_
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.1 — Homeodomain-like
Family Family familya.4.1.1 — Homeodomain

CATH v4.4 (1 domains)

Domain ID domain_id2lp0A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily60 — Homeodomain-like

8. Citations (1)

9. Files and Curves (10)