SAXSdb — 1bci

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

CYTOSOLIC PHOSPHOLIPASE A2

Homo sapiens

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 1–138	Fragment：C2 DOMAIN	CA CALCIUM ION × 2	SOLUTION NMR NMR measurement conditions：pH 7.1；308 K；Ionic strength (raw mmCIF value) 0.0；Pressure 1 NMR sample composition：20 MM TRIS, 0.5MM CACL2	Resolution not provided

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 1BCI	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CJY HUMAN CYTOSOLIC PHOSPHOLIPASE A2 Deposited 1999-04-20	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–749（749 aa）	Not recorded	CA CALCIUM ION × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；pH 8.5	Resolution 2.50 Å R-free 0.298
1CJY HUMAN CYTOSOLIC PHOSPHOLIPASE A2 Deposited 1999-04-20	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–749（749 aa）	Not recorded	CA CALCIUM ION × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；pH 8.5	Resolution 2.50 Å R-free 0.298
1RLW CALCIUM-PHOSPHOLIPID BINDING DOMAIN FROM CYTOSOLIC PHOSPHOLIPASE A2 Deposited 1997-10-28	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 17–141（125 aa） Fragment：C2 DOMAIN, RESIDUES 17 - 141 FROM CPLA2	Mutation：Y16S, C139A, C141S	CD CADMIUM ION × 2 CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；5-10MG/ML PROTEIN, 5MM CACL2, 1M SODIUM ACETATE, 0.1M HEPES (PH 7.5), 50MM CDSO4	Resolution 2.40 Å R-free 0.273

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PA24A_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–138； UniProt 1–138

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1bci
Deposition date deposition_date	1998-04-30
Structure title title	C2 DOMAIN OF CYTOSOLIC PHOSPHOLIPASE A2, NMR, MINIMIZED AVERAGE STRUCTURE
Keywords keywords	HYDROLASE, LIPID DEGRADATION, CYTOSOLIC PHOSPHOLIPASE A2, CALCIUM-DEPENDENT LIPID BINDING, C2 DOMAIN, PHOSPHOCHOLINE; HYDROLASE
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	16.30 Å
Radius of gyration Rg (electron density) rg_electron	15.21 Å
Forward intensity I(0) i0	3787470.00
Molecular weight molecular_weight	14189.0 kDa
Excluded volume excluded_volume	17856 Å³
Envelope volume envelope_volume	20413 Å³
Hydration-shell volume shell_volume	11900 Å³
Envelope diameter envelope_diameter	52.4 Å
Shell Rg shell_rg	20.29 Å
Envelope Rg envelope_rg	15.59 Å
Shape Rg shape_rg	15.18 Å
Total Rg total_rg	16.30 Å
Total atoms total_atoms	1967
Residues n_residues	123
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	54.1 Å
Rg (real space) rg_real	16.32 Å
Rg uncertainty (real space) rg_real_error	0.33 Å
I(0) (real space) i0_real	3.7870e+06
I(0) uncertainty (real space) i0_real_error	4.2160e+04
Rg (reciprocal space) rg_reciprocal	16.32 Å
I(0) (reciprocal space) i0_reciprocal	3787000.0000
Solution quality estimate total_estimate	0.8825
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	17.4 Å
Skewness Skewness skewness	0.373
Kurtosis Kurtosis kurtosis	-0.306
Angular range angular_range	— – 0.4900 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	765600.0000
Real-space data points n_real_points	79
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.839; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.969

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1bcia_
Class class	b — All beta proteins
Fold Fold fold	b.7 — C2 domain-like
Superfamily Superfamily superfamily	b.7.1 — C2 domain (Calcium/lipid-binding domain, CaLB)
Family Family family	b.7.1.1 — PLC-like (P variant)

CATH v4.4 (1 domains)

Domain ID domain_id	1bciA00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	150 — C2 domain

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	CYTOSOLIC PHOSPHOLIPASE A2
Molecular weight formula_weight	15971.1 kDa
EC 编号 ec_number	3.1.1.4
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1967

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

C2 DOMAIN OF CYTOSOLIC PHOSPHOLIPASE A2, NMR, MINIMIZED AVERAGE STRUCTURE

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

CYTOSOLIC PHOSPHOLIPASE A2

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 non-polymer

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	2

fit	/app/data/saxs_computation/bc/1bci/1bci.fit
pddf	/app/data/pr_computation/bc/1bci/1bci.pr.out
profile	/app/data/saxs_computation/bc/1bci/1bci.dat