SAXSdb — 1lp4

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

Protein kinase CK2

Zea mays

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	MAGNESIUM ION × 2 PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CSK2A_MAIZE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–332； UniProt 1–332

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	1lp4
Deposition date deposition_date	2002-05-07
Structure title title	Crystal structure of a binary complex of the catalytic subunit of protein kinase CK2 with Mg-AMPPNP
Keywords keywords	protein kinase, CK2, casein kinase 2, dual-cosubstrate specificity, TRANSFERASE; TRANSFERASE
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1lp4__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1lp4__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1lp4__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	21.45 Å
Rg (electron density)	20.30 Å
Total Rg	21.17 Å
Atom count	2760
Residues	327
Excluded volume	49185 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1lp4__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Protein kinase CK2
Molecular weight formula_weight	39291.2 kDa
EC 编号 ec_number	2.7.1.37
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	3047

MSKARVYADVNVLRPKEYWDYEALTVQWGEQDDYEVVRKVGRGKYSEVFEGINVNNNEKCIIKILKPVKKKKIKREIKILQNLCGGPNIVKLLDIVRDQHSKTPSLIFEYVNNTDFKVLYPTLTDYDIRYYIYELLKALDYCHSQGIMHRDVKPHNVMIDHELRKLRLIDWGLAEFYHPGKEYNVRVASRYFKGPELLVDLQDYDYSLDMWSLGCMFAGMIFRKEPFFYGHDNHDQLVKIAKVLGTDGLNVYLNKYRIELDPQLEALVGRHSRKPWLKFMNADNQHLVSPEAIDFLDKLLRYDHQERLTALEAMTHPYFQQVRAAENSRTRA

Source Source

Source organism organism	Zea mays
NCBI taxonomy ID ncbi_taxonomy_id	4577
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
Molecular weight formula_weight	506.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	287

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6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1lp4a_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamily	d.144.1 — Protein kinase-like (PK-like)
Family Family family	d.144.1.7 — Protein kinases, catalytic subunit

CATH v4.4 (2 domains)

Domain ID domain_id	1lp4A01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily	20 — Phosphorylase Kinase; domain 1

Domain ID domain_id	1lp4A02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily	10 — Transferase(Phosphotransferase) domain 1

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7. Citations (8)

;Inclining the purine base binding plane in protein kinase CK2 by exchanging the flanking side-chains generates a preference for ATP as a cosubstrate. ;

J.Mol.Biol. (2005)

PMID: 15740749 · DOI: 10.1016/j.jmb.2005.01.003 PRIMARY

Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme

Embo J. (2001)

PMID: 11574463 · DOI: 10.1093/emboj/20.19.5320

Crystallization and preliminary characterization of crystals of human protein kinase CK2

Acta Crystallogr.,Sect.D (2000)

PMID: 11092945 · DOI: 10.1107/S0907444900013627

GTP plus water mimic ATP in the active site of protein kinase CK2

NAT.STRUCT.BIOL. (1999)

PMID: 10581548 · DOI: 10.1038/70033

Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution

Embo J. (1998)

PMID: 9564028 · DOI: 10.1093/emboj/17.9.2451

Expression, purification and crystallization of the catalytic subunit of protein kinase CK2 from Zea mays

Acta Crystallogr.,Sect.D (1998)

PMID: 9761839 · DOI: 10.1107/S0907444997010184

Expression and characterization of a recombinant maize CK-2 alpha subunit

BIOCHIM.BIOPHYS.ACTA (1993)

PMID: 8485151 · DOI: 10.1016/0167-4781(93)90239-A

Cloning and sequencing of the casein kinase 2 alpha subunit from Zea mays

BIOCHIM.BIOPHYS.ACTA (1991)

PMID: 1756176 · DOI: 10.1016/0167-4781(91)90230-J

Unit-cell length a length_a	144.075 Å
Unit-cell length b length_b	59.624 Å
Unit-cell length c length_c	45.642 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	103.59 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	1.860 Å
Low-resolution limit resolution_low	55.000 Å
R factor r_factor	0.2073
R_work r_work	0.2060
R_free r_free	0.2437

Crystal structure of a binary complex of the catalytic subunit of protein kinase CK2 with Mg-AMPPNP

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

Protein kinase CK2

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1lp4__assembly_1__model_1

1lp4__assembly_1__model_1 | I(q)

1lp4__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

7. Citations (8)

Crystal structure of a binary complex of the catalytic subunit of protein kinase CK2 with Mg-AMPPNP

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

Protein kinase CK2

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1lp4__assembly_1__model_1

1lp4__assembly_1__model_1 | I(q)

1lp4__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

7. Citations (8)