SAXSdb — 1djh

▼

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

PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1

Rattus norvegicus

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 133–756	Mutation：DELTA(1-132) DELETION VARIANT	BA BARIUM ION × 3 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 5.2；pH 5.2	Resolution 2.50 Å R-free 0.270
2	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain B； UniProt 133–756	Mutation：DELTA(1-132) DELETION VARIANT	BA BARIUM ION × 3 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 5.2；pH 5.2	Resolution 2.50 Å R-free 0.270

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 1DJH	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1DJG PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT COMPLEXED WITH LANTHANUM Deposited 1996-09-25	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 133–756（624 aa）	Mutation：DEL(1-132) DELETION VARIANT	ACT ACETATE ION × 1 LA LANTHANUM (III) ION × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.60 Å R-free 0.270
1DJG PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT COMPLEXED WITH LANTHANUM Deposited 1996-09-25	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 133–756（624 aa）	Mutation：DEL(1-132) DELETION VARIANT	ACT ACETATE ION × 1 LA LANTHANUM (III) ION × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.60 Å R-free 0.270
1DJI PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT COMPLEXED WITH CALCIUM Deposited 1996-09-25	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 133–756（624 aa）	Mutation：DELTA(1-132) DELETION VARIANT	CA CALCIUM ION × 3 ACT ACETATE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.280
1DJI PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT COMPLEXED WITH CALCIUM Deposited 1996-09-25	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 133–756（624 aa）	Mutation：DELTA(1-132) DELETION VARIANT	CA CALCIUM ION × 3 ACT ACETATE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.280
1DJW PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT COMPLEXED WITH INOSITOL-2-METHYLENE-1,2-CYCLIC-MONOPHOSPHONATE Deposited 1996-08-24	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 133–756（624 aa）	Mutation：DELTA(1-132) DELETION VARIANT	CA CALCIUM ION × 3 ACT ACETATE ION × 1 CIP INOSITOL-2-METHYLENE-1,2-CYCLIC-MONOPHOSPHATE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.45 Å R-free 0.270
1DJW PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT COMPLEXED WITH INOSITOL-2-METHYLENE-1,2-CYCLIC-MONOPHOSPHONATE Deposited 1996-08-24	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 133–756（624 aa）	Mutation：DELTA(1-132) DELETION VARIANT	CA CALCIUM ION × 3 ACT ACETATE ION × 1 CIP INOSITOL-2-METHYLENE-1,2-CYCLIC-MONOPHOSPHATE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.45 Å R-free 0.270
1DJX PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT COMPLEXED WITH INOSITOL-1,4,5-TRISPHOSPHATE Deposited 1996-08-24	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 133–756（624 aa）	Mutation：DELTA(1-132) DELETION VARIANT	CA CALCIUM ION × 2 ACT ACETATE ION × 1 I3P D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å R-free 0.270
1DJX PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT COMPLEXED WITH INOSITOL-1,4,5-TRISPHOSPHATE Deposited 1996-08-24	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 133–756（624 aa）	Mutation：DELTA(1-132) DELETION VARIANT	CA CALCIUM ION × 2 ACT ACETATE ION × 1 I3P D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å R-free 0.270
1DJY PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT COMPLEXED WITH INOSITOL-2,4,5-TRISPHOSPHATE Deposited 1996-08-24	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 133–756（624 aa）	Mutation：DELTA(1-132) DELETION VARIANT	CA CALCIUM ION × 3 ACT ACETATE ION × 1 I2P D-MYO-INOSITOL-2,4,5-TRIPHOSPHATE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å R-free 0.260
1DJY PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT COMPLEXED WITH INOSITOL-2,4,5-TRISPHOSPHATE Deposited 1996-08-24	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 133–756（624 aa）	Mutation：DELTA(1-132) DELETION VARIANT	CA CALCIUM ION × 3 ACT ACETATE ION × 1 I2P D-MYO-INOSITOL-2,4,5-TRIPHOSPHATE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å R-free 0.260
1DJZ PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT COMPLEXED WITH INOSITOL-4,5-BISPHOSPHATE Deposited 1996-08-24	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 133–756（624 aa）	Mutation：DELTA(1-132) DELETION VARIANT	CA CALCIUM ION × 2 ACT ACETATE ION × 1 IP2 D-MYO-INOSITOL-4,5-BISPHOSPHATE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.95 Å R-free 0.270
1DJZ PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT COMPLEXED WITH INOSITOL-4,5-BISPHOSPHATE Deposited 1996-08-24	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 133–756（624 aa）	Mutation：DELTA(1-132) DELETION VARIANT	CA CALCIUM ION × 2 ACT ACETATE ION × 1 IP2 D-MYO-INOSITOL-4,5-BISPHOSPHATE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.95 Å R-free 0.270
1MAI STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM PHOSPHOLIPASE C DELTA IN COMPLEX WITH INOSITOL TRISPHOSPHATE Deposited 1996-05-23	Different construct 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 11–140（130 aa） Fragment：PLECKSTRIN HOMOLOGY DOMAIN	Not recorded	I3P D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；pH 6.5	Resolution 1.90 Å R-free 0.291
1QAS 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA 1 Deposited 1996-08-02	Different construct 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 135–756（622 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions clusters formed by mixing - used as seeds in hanging drops；pH 6.5；NEEDLE CLUSTERS WERE FORMED BY MIXING EQUAL VOLUMES OF PROTEIN SOLUTION (22 MG/ML) WITH A WELL SOLUTION CONSISTING OF 0.1 M NA MES (PH 6.0), 0.2 M LICL, 20% GLYCEROL, AND 12-14 % PEG 8000. FRAGMENTS OF THE NEEDLE CLUSTERS WERE USED TO SEED HANGING DROPS. THE WELL SOLUTION USED FOR THE SEEDING EXPERIMENTS WAS ADJUSTED TO 0.1M NA MES (PH 6.5), 0.2 M LICL, 20 % GLYCEROL, AND 6-8 % PEG 8000., clusters formed by mixing - used as seeds in hanging drops	Resolution 2.40 Å R-free 0.286
1QAS 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA 1 Deposited 1996-08-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 135–756（622 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions clusters formed by mixing - used as seeds in hanging drops；pH 6.5；NEEDLE CLUSTERS WERE FORMED BY MIXING EQUAL VOLUMES OF PROTEIN SOLUTION (22 MG/ML) WITH A WELL SOLUTION CONSISTING OF 0.1 M NA MES (PH 6.0), 0.2 M LICL, 20% GLYCEROL, AND 12-14 % PEG 8000. FRAGMENTS OF THE NEEDLE CLUSTERS WERE USED TO SEED HANGING DROPS. THE WELL SOLUTION USED FOR THE SEEDING EXPERIMENTS WAS ADJUSTED TO 0.1M NA MES (PH 6.5), 0.2 M LICL, 20 % GLYCEROL, AND 6-8 % PEG 8000., clusters formed by mixing - used as seeds in hanging drops	Resolution 2.40 Å R-free 0.286
1QAT 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA COMPLEX WITH SAMARIUM (III) CHLORIDE Deposited 1996-08-02	Different construct 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 135–756（622 aa）	Not recorded	SM SAMARIUM (III) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions clusters formed by mixing - used as seeds in hanging drops；pH 6.5；NEEDLE CLUSTERS WERE FORMED BY MIXING EQUAL VOLUMES OF PROTEIN SOLUTION (22 MG/ML) WITH A WELL SOLUTION CONSISTING OF 0.1 M NA MES (PH 6.0), 0.2 M LICL, 20% GLYCEROL, AND 12-14 % PEG 8000. FRAGMENTS OF THE NEEDLE CLUSTERS WERE USED TO SEED HANGING DROPS. THE WELL SOLUTION USED FOR THE SEEDING EXPERIMENTS WAS ADJUSTED TO 0.1M NA MES (PH 6.5), 0.2 M LICL, 20 % GLYCEROL, AND 6-8 % PEG 8000., clusters formed by mixing - used as seeds in hanging drops	Resolution 3.00 Å R-free 0.261
1QAT 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA COMPLEX WITH SAMARIUM (III) CHLORIDE Deposited 1996-08-02	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 135–756（622 aa）	Not recorded	SM SAMARIUM (III) ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions clusters formed by mixing - used as seeds in hanging drops；pH 6.5；NEEDLE CLUSTERS WERE FORMED BY MIXING EQUAL VOLUMES OF PROTEIN SOLUTION (22 MG/ML) WITH A WELL SOLUTION CONSISTING OF 0.1 M NA MES (PH 6.0), 0.2 M LICL, 20% GLYCEROL, AND 12-14 % PEG 8000. FRAGMENTS OF THE NEEDLE CLUSTERS WERE USED TO SEED HANGING DROPS. THE WELL SOLUTION USED FOR THE SEEDING EXPERIMENTS WAS ADJUSTED TO 0.1M NA MES (PH 6.5), 0.2 M LICL, 20 % GLYCEROL, AND 6-8 % PEG 8000., clusters formed by mixing - used as seeds in hanging drops	Resolution 3.00 Å R-free 0.261
2ISD PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT Deposited 1997-03-31	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 133–756（624 aa）	Mutation：DELTA(1-132) DELETION VARIANT	ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.8；pH 5.8	Resolution 2.50 Å R-free 0.280
2ISD PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT Deposited 1997-03-31	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 133–756（624 aa）	Mutation：DELTA(1-132) DELETION VARIANT	ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.8；pH 5.8	Resolution 2.50 Å R-free 0.280

10 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PLCD1_RAT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–624； UniProt 133–756 Author chain B； PDBConstruct 1–624； UniProt 133–756

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1djh
Deposition date deposition_date	1996-09-25
Structure title title	PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT COMPLEXED WITH BARIUM
Keywords keywords	PHOSPHORIC DIESTER HYDROLASE, HYDROLASE, LIPID DEGRADATION, TRANSDUCER, CALCIUM-BINDING, PHOSPHOLIPASE C, PHOSPHOINOSITIDE-SPECIFIC; LIPID DEGRADATION
Experimental Method method	X-RAY DIFFRACTION

▼

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

Radius of gyration Rg (Guinier) rg_guinier	41.80 Å
Radius of gyration Rg (electron density) rg_electron	42.09 Å
Forward intensity I(0) i0	230829000.00
Molecular weight molecular_weight	121800.0 kDa
Excluded volume excluded_volume	151270 Å³
Envelope volume envelope_volume	199280 Å³
Hydration-shell volume shell_volume	42796 Å³
Envelope diameter envelope_diameter	158.8 Å
Shell Rg shell_rg	42.56 Å
Envelope Rg envelope_rg	42.23 Å
Shape Rg shape_rg	42.04 Å
Total Rg total_rg	42.27 Å
Total atoms total_atoms	8514
Residues n_residues	1071
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

▼

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

Maximum dimension Dmax dmax	151.5 Å
Rg (real space) rg_real	42.26 Å
Rg uncertainty (real space) rg_real_error	1.87 Å
I(0) (real space) i0_real	2.3080e+08
I(0) uncertainty (real space) i0_real_error	4.5350e+06
Rg (reciprocal space) rg_reciprocal	41.81 Å
I(0) (reciprocal space) i0_reciprocal	230700000.0000
Solution quality estimate total_estimate	0.7976
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	35.9 Å
Skewness Skewness skewness	0.591
Kurtosis Kurtosis kurtosis	-0.217
Angular range angular_range	— – 0.1900 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	25200000.0000
Real-space data points n_real_points	39
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.625; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.680; Smooth: 0.811

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1
Molecular weight formula_weight	70574.5 kDa
EC 编号 ec_number	3.1.4.11
Mutation mutation	DELTA(1-132) DELETION VARIANT
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	9257

GSMDQRQKLQHWIHSCLRKADKNKDNKMNFKELKDFLKELNIQVDDGYARKIFRECDHSQTDSLEDEEIETFYKMLTQRAEIDRAFEEAAGSAETLSVERLVTFLQHQQREEEAGPALALSLIERYEPSETAKAQRQMTKDGFLMYLLSADGNAFSLAHRRVYQDMDQPLSHYLVSSSHNTYLLEDQLTGPSSTEAYIRALCKGCRCLELDCWDGPNQEPIIYHGYTFTSKILFCDVLRAIRDYAFKASPYPVILSLENHCSLEQQRVMARHLRAILGPILLDQPLDGVTTSLPSPEQLKGKILLKGKKLGGLLPAGGENGSEATDVSDEVEAAEMEDEAVRSQVQHKPKEDKLKLVPELSDMIIYCKSVHFGGFSSPGTSGQAFYEMASFSESRALRLLQESGNGFVRHNVSCLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNFQTPGPEMDVYLGCFQDNGGCGYVLKPAFLRDPNTTFNSRALTQGPWWRPERLRVRIISGQQLPKVNKNKNSIVDPKVIVEIHGVGRDTGSRQTAVITNNGFNPRWDMEFEFEVTVPDLALVRFMVEDYDSSSKNDFIGQSTIPWNSLKQGYRHVHLLSKNGDQHPSATLFVKISIQD

来源 Source

来源生物 organism	Rattus norvegicus
通用名 common_name	Norway rat
NCBI Class编号 ncbi_taxonomy_id	10116
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	BARIUM ION
Molecular weight formula_weight	137.3 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 3 Entity 3 non-polymer

Description description	ACETATE ION
Molecular weight formula_weight	59.0 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	742

▼

7. Fold Classification (SCOP + CATH) 13 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d1djha1
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.1 — EF-hand
Family Family family	a.39.1.7 — EF-hand modules in multidomain proteins

Domain ID domain_id	d1djha2
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)

Domain ID domain_id	d1djha3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.18 — PLC-like phosphodiesterases
Family Family family	c.1.18.1 — Mammalian PLC

Domain ID domain_id	d1djhb1
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.1 — EF-hand
Family Family family	a.39.1.7 — EF-hand modules in multidomain proteins

Domain ID domain_id	d1djhb2
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)

Domain ID domain_id	d1djhb3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.18 — PLC-like phosphodiesterases
Family Family family	c.1.18.1 — Mammalian PLC

CATH v4.4 (7 domains)

Domain ID domain_id	1djhA01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	1djhA02
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	190 — Phosphatidylinositol (PI) phosphodiesterase

Domain ID domain_id	1djhA03
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	150 — C2 domain

Domain ID domain_id	1djhB01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	1djhB02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

Domain ID domain_id	1djhB03
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	190 — Phosphatidylinositol (PI) phosphodiesterase

Domain ID domain_id	1djhB04
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	150 — C2 domain

▶

8. Citations (1)

▶

Unit-cell length a length_a	398.250 Å
Unit-cell length b length_b	398.250 Å
Unit-cell length c length_c	398.250 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	192

Space group space_group	F 41 3 2
Space-group number int_tables_number	210
Crystal system crystal_system	—

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	—
R_work r_work	0.2100
R_free r_free	0.2700

fit	/app/data/saxs_computation/dj/1djh/1djh.fit
pddf	/app/data/pr_computation/dj/1djh/1djh.pr.out
profile	/app/data/saxs_computation/dj/1djh/1djh.dat

PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT COMPLEXED WITH BARIUM

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

PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1

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

Refinement Refinement

Diffraction experiment Diffraction