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1b8l

Calcium-bound D51A/E101D/F102W Triple Mutant of Beta Carp Parvalbumin

Method: X-RAY DIFFRACTION Dmax: 42.8 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (PARVALBUMIN)

Cyprinus carpio

UniProt P02618

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 1–108 Mutation：D51A, E101D, F102W CO3 CARBONATE ION × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.9；CRYSTALLIZATION CONDITIONS 40% PEG 4000, 50 MM CACL2, 50 M PH 7.0, 4 DEGREES C, pH 6.9 Resolution 1.70 Å R-free 0.227

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.

Other PDB Difference from Current Entry 1B8L Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1B8C PARVALBUMIN Deposited 1999-01-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–108（108 aa）
Chain B 1–108（108 aa）
Mutation：D51A, E101D, F102W Mutation：D51A, E101D, F102W MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；CRYSTALLIZATION CONDITIONS: 40% PEG 4000, 200 MM MGCL2, 50 M PH 7. THE CRYSTALS WERE GROWN AT 4 DEGREES C., pH 7.0
Resolution 2.00 Å R-free 0.300
1B8R PARVALBUMIN Deposited 1999-02-02 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–108（108 aa）
Mutation：F102W CA CALCIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；CRYSTALLIZATION CONDITIONS: PH 5.0 - 5.5, 3.1 - 3.2 M AMMONIUM SULFATE 0.05 - 0.10 M CACL2, ROOM TEMPERATURE, pH 7.0
Resolution 1.90 Å R-free 0.270
1B9A PARVALBUMIN (MUTATION;D51A, F102W) Deposited 1999-02-10 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–108（108 aa）
Mutation：D51A, F102W CA CALCIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；pH 7.0
Resolution 2.00 Å R-free 0.290
1CDP RESTRAINED LEAST SQUARES REFINEMENT OF NATIVE (CALCIUM) AND CADMIUM-SUBSTITUTED CARP PARVALBUMIN USING X-RAY CRYSTALLOGRAPHIC DATA AT 1.6-ANGSTROMS RESOLUTION Deposited 1990-01-24 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–108（108 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CD CADMIUM ION × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.60 Å
4CPV REFINED CRYSTAL STRUCTURE OF CALCIUM-LIGANDED CARP PARVALBUMIN 4.25 AT 1.5-ANGSTROMS RESOLUTION Deposited 1989-10-18 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–108（108 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.50 Å
5CPV RESTRAINED LEAST SQUARES REFINEMENT OF NATIVE (CALCIUM) AND CADMIUM-SUBSTITUTED CARP PARVALBUMIN USING X-RAY CRYSTALLOGRAPHIC DATA AT 1.6-ANGSTROMS RESOLUTION Deposited 1990-01-24 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–108（108 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.60 Å

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRVB_CYPCA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–108； UniProt 1–108

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 1b8l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1b8l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1b8l
Deposition date deposition_date1999-02-01
Structure title titleCalcium-bound D51A/E101D/F102W Triple Mutant of Beta Carp Parvalbumin
Keywords keywordsCALCIUM BINDING PROTEIN, EF-HAND PROTEINS, PARVALBUMIN, CALCIUM-BINDING; CALCIUM BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier14.28 Å
Radius of gyration Rg (electron density) rg_electron12.62 Å
Forward intensity I(0) i02724950.00
Molecular weight molecular_weight11512.0 kDa
Excluded volume excluded_volume14433 ų
Envelope volume envelope_volume15750 ų
Hydration-shell volume shell_volume10686 ų
Envelope diameter envelope_diameter39.1 Å
Shell Rg shell_rg18.36 Å
Envelope Rg envelope_rg12.82 Å
Shape Rg shape_rg12.56 Å
Total Rg total_rg14.09 Å
Total atoms total_atoms811
Residues n_residues108
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax42.8 Å
Rg (real space) rg_real14.14 Å
Rg uncertainty (real space) rg_real_error0.21 Å
I(0) (real space) i0_real2.7250e+06
I(0) uncertainty (real space) i0_real_error2.9550e+04
Rg (reciprocal space) rg_reciprocal14.15 Å
I(0) (reciprocal space) i0_reciprocal2725000.0000
Solution quality estimate total_estimate0.7519
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.3 Å
Skewness Skewness skewness-0.017
Kurtosis Kurtosis kurtosis-0.424
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha331300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.910; Stabil: 1.000; Sysdev: 0.368; Positv: 1.000; Valcen: 0.976; Smooth: 0.962
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1b8la_
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.4 — Parvalbumin

CATH v4.4 (1 domains)

Domain ID domain_id1b8lA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
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8. Citations (2)

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9. Files and Curves (10)