1u2m

Crystal Structure of Skp

Method: X-RAY DIFFRACTION Dmax: 90.5 Å Quality: GOOD

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

Histone-like protein HLP-1

Escherichia coli

UniProt P0AEU7

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 homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 21–161 Chain B; UniProt 21–161 Chain C; UniProt 21–161 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;277 K;PEG 350 monomethy ether, ammonium dihydrogen phosphate, Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.30 Å R-free 0.259

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 HLPA_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–143; UniProt 21–161 Author chain B; PDBConstruct 3–143; UniProt 21–161 Author chain C; PDBConstruct 3–143; UniProt 21–161

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 1u2m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1u2m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1u2m
Deposition date deposition_date2004-07-19
Structure title titleCrystal Structure of Skp
Keywords keywordscoiled coil, chaperone; CHAPERONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.92
Radius of gyration Rg (electron density) rg_electron27.14
Forward intensity I(0) i027418900.00
Molecular weight molecular_weight37845.0 kDa
Excluded volume excluded_volume46379 ų
Envelope volume envelope_volume70298 ų
Hydration-shell volume shell_volume22694 ų
Envelope diameter envelope_diameter93.8
Shell Rg shell_rg32.67
Envelope Rg envelope_rg26.38
Shape Rg shape_rg27.04
Total Rg total_rg28.07
Total atoms total_atoms2615
Residues n_residues335
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 dmax90.5
Rg (real space) rg_real27.96
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real2.7420e+07
I(0) uncertainty (real space) i0_real_error4.2330e+05
Rg (reciprocal space) rg_reciprocal27.95
I(0) (reciprocal space) i0_reciprocal27420000.0000
Solution quality estimate total_estimate0.8815
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.5
Skewness Skewness skewness0.316
Kurtosis Kurtosis kurtosis-0.279
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1709000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.877; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.847

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (5 domains)

Domain ID domain_idd1u2ma1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.48 — OmpH-like
Superfamily Superfamily superfamilyf.48.1 — OmpH-like
Family Family familyf.48.1.1 — OmpH-like
Domain ID domain_idd1u2ma2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1u2mb_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.48 — OmpH-like
Superfamily Superfamily superfamilyf.48.1 — OmpH-like
Family Family familyf.48.1.1 — OmpH-like
Domain ID domain_idd1u2mc1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.48 — OmpH-like
Superfamily Superfamily superfamilyf.48.1 — OmpH-like
Family Family familyf.48.1.1 — OmpH-like
Domain ID domain_idd1u2mc2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (3 domains)

Domain ID domain_id1u2mA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology910 — Protein Binding, DinI Protein; Chain A
Homologous superfamily homologous superfamily20 — Skp domain
Domain ID domain_id1u2mB00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology910 — Protein Binding, DinI Protein; Chain A
Homologous superfamily homologous superfamily20 — Skp domain
Domain ID domain_id1u2mC00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology910 — Protein Binding, DinI Protein; Chain A
Homologous superfamily homologous superfamily20 — Skp domain

8. Citations (1)

9. Files and Curves (10)