2pzg

Minimal human CFTR first nucleotide binding domain as a monomer

Method: X-RAY DIFFRACTION Dmax: 75.8 Å Quality: EXCELLENT

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

Cystic fibrosis transmembrane conductance regulator

Homo sapiens

UniProt P13569

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 375–404 Chain A; UniProt 437–646 Fragment:CFTR NBD1 375-646(del405-436) Mutation:del405-436 MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6.5;281 K;Protein: 9.5mg/ml NBD1, 0.15M NaCl, 0.01M methionine, 0.01M HEPES pH 7.5, 10% glycerol, 0.001M TCEP, 0.002M ATP; Well: 0.1M Hepes pH 6.5, 25% PEG 10K ; Cryo: 25% glycerol, vapor diffusion, temperature 281K Resolution 1.80 Å R-free 0.234
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 375–404 Chain B; UniProt 437–646 Fragment:CFTR NBD1 375-646(del405-436) Mutation:del405-436 MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6.5;281 K;Protein: 9.5mg/ml NBD1, 0.15M NaCl, 0.01M methionine, 0.01M HEPES pH 7.5, 10% glycerol, 0.001M TCEP, 0.002M ATP; Well: 0.1M Hepes pH 6.5, 25% PEG 10K ; Cryo: 25% glycerol, vapor diffusion, temperature 281K Resolution 1.80 Å R-free 0.234

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.

52 other PDB entries and 69 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CFTR_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–31; UniProt 375–404 Author chain A; PDBConstruct 32–241; UniProt 437–646 Author chain B; PDBConstruct 2–31; UniProt 375–404 Author chain B; PDBConstruct 32–241; UniProt 437–646

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 2pzg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2pzg
Deposition date deposition_date2007-05-18
Structure title titleMinimal human CFTR first nucleotide binding domain as a monomer
Keywords keywordsNBD, ABC transporter, CFTR, Hydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.05
Radius of gyration Rg (electron density) rg_electron24.15
Forward intensity I(0) i040576400.00
Molecular weight molecular_weight48954.0 kDa
Excluded volume excluded_volume61229 ų
Envelope volume envelope_volume74473 ų
Hydration-shell volume shell_volume25831 ų
Envelope diameter envelope_diameter77.2
Shell Rg shell_rg31.04
Envelope Rg envelope_rg24.11
Shape Rg shape_rg24.17
Total Rg total_rg24.92
Total atoms total_atoms3426
Residues n_residues438
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 dmax75.8
Rg (real space) rg_real24.97
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real4.0580e+07
I(0) uncertainty (real space) i0_real_error5.5300e+05
Rg (reciprocal space) rg_reciprocal25.00
I(0) (reciprocal space) i0_reciprocal40580000.0000
Solution quality estimate total_estimate0.9132
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.6
Skewness Skewness skewness0.177
Kurtosis Kurtosis kurtosis-0.622
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8528000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.974; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.945

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2pzga_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.12 — ABC transporter ATPase domain-like
Domain ID domain_idd2pzgb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.12 — ABC transporter ATPase domain-like

CATH v4.4 (2 domains)

Domain ID domain_id2pzgA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id2pzgB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (2)

9. Files and Curves (10)