SAXSdb — 3c50

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

Rhodopsin kinase

Bos taurus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	MAGNESIUM ION × 4 CHLORIDE ION × 8 ADENOSINE-5'-DIPHOSPHATE × 2 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	RK_BOVIN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–535； UniProt 1–535 Author chain B； PDBConstruct 1–535； UniProt 1–535

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	3c50
Deposition date deposition_date	2008-01-30
Structure title title	Crystal Structure of G protein coupled receptor kinase 1 bound to ADP and magnesium chloride at 2.6A
Keywords keywords	;Ser/Thr kinase, RGS homology domain, G protein coupled receptor kinase, GRK, GRK1, rhodopsin kinase, P-loop, autophosphorylation, ADP, ATP-binding, Lipoprotein, Membrane, Methylation, Nucleotide-binding, Phosphoprotein, Prenylation, Serine/threonine-protein kinase, 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.

3c50__assembly_1__model_1

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

Download this curve (.dat)

3c50__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3c50__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	41.49 Å
Rg (electron density)	41.67 Å
Total Rg	41.80 Å
Atom count	8067
Residues	995
Excluded volume	143790 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3c50__assembly_1__model_1`	dimeric （2）	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 (6)

Entity 1 Entity 1 polymer

Description description	Rhodopsin kinase
Molecular weight formula_weight	61429.9 kDa
EC 编号 ec_number	2.7.11.14
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	8438

MDFGSLETVVANSAFIAARGSFDASSGPASRDRKYLARLKLPPLSKCEALRESLDLGFEGMCLEQPIGKRLFQQFLRTHEQHGPALQLWKDIEDYDTADDALRPQKAQALRAAYLEPQAQLFCSFLDAETVARARAGAGDGLFQPLLRAVLAHLGQAPFQEFLDSLYFLRFLQWKWLEAQPMGEDWFLDFRVLGRGGFGEVFACQMKATGKLYACKKLNKKRLKKRKGYQGAMVEKKILAKVHSRFIVSLAYAFETKTDLCLVMTIMNGGDIRYHIYNVDEDNPGFQEPRAIFYTAQIVSGLEHLHQRNIIYRDLKPENVLLDDDGNVRISDLGLAVELKAGQTKTKGYAGTPGFMAPELLLGEEYDFSVDYFALGVTLYEMIAARGPFRARGEKVENKELKQRVLEQAVTYPDKFSPASKDFCEALLQKDPEKRLGFRDGSCDGLRTHPLFRDISWRQLEAGMLTPPFVPDSRTVYAKNIQDVGAFSTVKGVAFEKADTEFFQEFASGTCPIPWQEEMIETGVFGDLNVWRPDGVDHHHHHH

Source Source

Source organism organism	Bos taurus
Common name common_name	cattle
NCBI taxonomy ID ncbi_taxonomy_id	9913
Host organism host_organism	Trichoplusia ni

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	4

Entity 3 Entity 3 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 4 Entity 4 non-polymer

Description description	ADENOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	427.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 non-polymer

Description description	2-(N-MORPHOLINO)-ETHANESULFONIC ACID
Molecular weight formula_weight	195.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	303

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6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id	3c50A01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	167 — Regulator of G-protein Signalling 4; domain 2
Homologous superfamily homologous superfamily	10 — Regulator of G-protein Signalling 4, domain 2

Domain ID domain_id	3c50A02
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	3c50A03
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

Domain ID domain_id	3c50B01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	167 — Regulator of G-protein Signalling 4; domain 2
Homologous superfamily homologous superfamily	10 — Regulator of G-protein Signalling 4, domain 2

Domain ID domain_id	3c50B02
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	3c50B03
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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Unit-cell length a length_a	65.504 Å
Unit-cell length b length_b	122.304 Å
Unit-cell length c length_c	174.076 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	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.600 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.1898
R_work r_work	0.1898
R_free r_free	—

Crystal Structure of G protein coupled receptor kinase 1 bound to ADP and magnesium chloride at 2.6A

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

Rhodopsin kinase

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

3c50__assembly_1__model_1

3c50__assembly_1__model_1 | I(q)

3c50__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 (6)

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 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

7. Citations (1)

Crystal Structure of G protein coupled receptor kinase 1 bound to ADP and magnesium chloride at 2.6A

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

Rhodopsin kinase

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

3c50__assembly_1__model_1

3c50__assembly_1__model_1 | I(q)

3c50__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 (6)

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 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

7. Citations (1)