6l2d

Crystal structure of a cupin protein (tm1459) in copper (Cu) substituted form

Method: X-RAY DIFFRACTION Dmax: 60.1 Å Quality: REASONABLE

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

Cupin_2 domain-containing protein

Thermotoga maritima MSB8

UniProt Q9X1H0

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–114 Chain B; UniProt 1–114 Non-standard monomer:Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;25%(w/v) Jeffamine ED-2001, 0.1M MES Resolution 1.20 Å R-free 0.186

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.

21 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9X1H0_THEMA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–118; UniProt 1–114 Author chain B; PDBConstruct 5–118; UniProt 1–114

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 6l2d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6l2d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6l2d
Deposition date deposition_date2019-10-03
Structure title titleCrystal structure of a cupin protein (tm1459) in copper (Cu) substituted form
Keywords keywordsArtificial metalloenzymes, Copper enzyme, Cupin, METAL BINDING PROTEIN; METAL BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.65
Radius of gyration Rg (electron density) rg_electron17.20
Forward intensity I(0) i011981000.00
Molecular weight molecular_weight26139.0 kDa
Excluded volume excluded_volume32818 ų
Envelope volume envelope_volume36571 ų
Hydration-shell volume shell_volume17717 ų
Envelope diameter envelope_diameter59.9
Shell Rg shell_rg23.49
Envelope Rg envelope_rg17.46
Shape Rg shape_rg17.19
Total Rg total_rg18.19
Total atoms total_atoms3639
Residues n_residues230
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 dmax60.1
Rg (real space) rg_real18.56
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real1.1980e+07
I(0) uncertainty (real space) i0_real_error1.5790e+05
Rg (reciprocal space) rg_reciprocal18.57
I(0) (reciprocal space) i0_reciprocal11980000.0000
Solution quality estimate total_estimate0.7063
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.2
Skewness Skewness skewness0.214
Kurtosis Kurtosis kurtosis-0.367
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2516000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.866; Stabil: 1.000; Sysdev: 0.197; Positv: 1.000; Valcen: 0.998; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd6l2da1
Class classb — All beta proteins
Fold Fold foldb.82 — Double-stranded beta-helix
Superfamily Superfamily superfamilyb.82.1 — RmlC-like cupins
Family Family familyb.82.1.10 — TM1459-like
Domain ID domain_idd6l2da2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd6l2db_
Class classb — All beta proteins
Fold Fold foldb.82 — Double-stranded beta-helix
Superfamily Superfamily superfamilyb.82.1 — RmlC-like cupins
Family Family familyb.82.1.10 — TM1459-like

CATH v4.4 (2 domains)

Domain ID domain_id6l2dA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily10 — Jelly Rolls
Domain ID domain_id6l2dB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily10 — Jelly Rolls

8. Citations (1)

9. Files and Curves (10)