2rkm

STRUCTURE OF OPPA COMPLEXED WITH LYS-LYS

Method: X-RAY DIFFRACTION Dmax: 84.2 Å Quality: GOOD

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 26–542 Not recorded LYS LYSINE × 2 IUM URANYL (VI) ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.5;7% PEG 4K, 50MM SODIUM ACETATE PH5.5, 1MM URANYL ACETATE AND 30MG/ML OPPA Resolution 1.80 Å R-free 0.219

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 2rkm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2rkm
Deposition date deposition_date1997-03-25
Structure title titleSTRUCTURE OF OPPA COMPLEXED WITH LYS-LYS
Keywords keywordsPEPTIDE TRANSPORT, COMPLEX (BINDING PROTEIN-DIPEPTIDE), Peptide BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.76
Radius of gyration Rg (electron density) rg_electron23.46
Forward intensity I(0) i065487500.00
Molecular weight molecular_weight61222.0 kDa
Excluded volume excluded_volume74970 ų
Envelope volume envelope_volume86854 ų
Hydration-shell volume shell_volume30221 ų
Envelope diameter envelope_diameter81.6
Shell Rg shell_rg31.26
Envelope Rg envelope_rg23.57
Shape Rg shape_rg23.26
Total Rg total_rg24.84
Total atoms total_atoms4207
Residues n_residues517
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 dmax84.2
Rg (real space) rg_real24.63
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real6.5490e+07
I(0) uncertainty (real space) i0_real_error1.0050e+06
Rg (reciprocal space) rg_reciprocal24.66
I(0) (reciprocal space) i0_reciprocal65490000.0000
Solution quality estimate total_estimate0.7907
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary30.7
Skewness Skewness skewness0.225
Kurtosis Kurtosis kurtosis-0.398
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9605000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.768; Stabil: 0.992; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2rkma_
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_id2rkmA01
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_id2rkmA02
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_id2rkmA03
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 (5)

9. Files and Curves (10)