2olb

OLIGOPEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH TRI-LYSINE

Method: X-RAY DIFFRACTION Dmax: 76.7 Å Quality: REASONABLE

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

OLIGO-PEPTIDE BINDING PROTEIN

OrganismNot specified

UniProt P06202

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 26–542 Not recorded TRIPEPTIDE LYS-LYS-LYS × 1 IUM URANYL (VI) ION × 8 ACT ACETATE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.5;pH 5.5 Resolution 1.40 Å

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 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name OPPA_SALTY
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–517; UniProt 26–542

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 2olb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2olb
Deposition date deposition_date1995-09-10
Structure title titleOLIGOPEPTIDE BINDING PROTEIN (OPPA) COMPLEXED WITH TRI-LYSINE
Keywords keywordsPERIPLASMIC, COMPLEX (BINDING PROTEIN-PEPTIDE) COMPLEX; COMPLEX (BINDING PROTEIN/PEPTIDE)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.36
Radius of gyration Rg (electron density) rg_electron23.10
Forward intensity I(0) i065954700.00
Molecular weight molecular_weight61624.0 kDa
Excluded volume excluded_volume75500 ų
Envelope volume envelope_volume84053 ų
Hydration-shell volume shell_volume29629 ų
Envelope diameter envelope_diameter80.6
Shell Rg shell_rg30.93
Envelope Rg envelope_rg23.27
Shape Rg shape_rg22.91
Total Rg total_rg24.47
Total atoms total_atoms4235
Residues n_residues520
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 dmax76.7
Rg (real space) rg_real24.23
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real6.5950e+07
I(0) uncertainty (real space) i0_real_error9.4080e+05
Rg (reciprocal space) rg_reciprocal24.26
I(0) (reciprocal space) i0_reciprocal65960000.0000
Solution quality estimate total_estimate0.7305
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.2
Skewness Skewness skewness0.220
Kurtosis Kurtosis kurtosis-0.390
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8965000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.903; Stabil: 1.000; Sysdev: 0.264; Positv: 1.000; Valcen: 0.998; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2olba_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamilyc.94.1 — Periplasmic binding protein-like II
Family Family familyc.94.1.1 — Phosphate binding protein-like

CATH v4.4 (3 domains)

Domain ID domain_id2olbA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id2olbA02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology76 — Dipeptide-binding Protein; domain 1
Homologous superfamily homologous superfamily10 — Dipeptide-binding Protein; Domain 1
Domain ID domain_id2olbA03
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology105 — Dipeptide-binding Protein; domain 3
Homologous superfamily homologous superfamily10 — Dipeptide-binding Protein; Domain 3

8. Citations (3)

9. Files and Curves (10)