SAXSdb — 2jj4

▼

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

ACETYLGLUTAMATE KINASE

SYNECHOCOCCUS ELONGATUS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 12	NITROGEN REGULATORY PROTEIN P-II × 6 （P0A3F4） N-ACETYL-L-GLUTAMATE × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ARGB_SYNP7
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 21–321； UniProt 1–301 Author chain B； PDBConstruct 21–321； UniProt 1–301 Author chain C； PDBConstruct 21–321； UniProt 1–301

NITROGEN REGULATORY PROTEIN P-II

SYNECHOCOCCUS ELONGATUS

UniProt P0A3F4

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 12	ACETYLGLUTAMATE KINASE × 6 （Q6V1L5） N-ACETYL-L-GLUTAMATE × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	GLNB_SYNP7
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain D； PDBConstruct 1–112； UniProt 1–112 Author chain E； PDBConstruct 1–112； UniProt 1–112 Author chain F； PDBConstruct 1–112； UniProt 1–112

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	2jj4
Deposition date deposition_date	2007-07-04
Structure title title	The complex of PII and acetylglutamate kinase from Synechococcus elongatus PCC7942
Keywords keywords	;TRANSFERASE, CYANOBACTERIA, TRANSCRIPTION, ACETYLGLUTAMATE, PHOSPHORYLATION, PII SIGNAL PROTEIN, TRANSCRIPTION REGULATION, N-ACETYL-L-GLUTAMATE KINASE, NUCLEOTIDE-BINDING, ARGININE INHIBITION, ARGININE BIOSYNTHESIS, AMINO-ACID BIOSYNTHESIS, GLNB, KINASE, TRIMER, HEXAMER, ATP-BINDING ;; TRANSCRIPTION
Experimental Method method	X-RAY DIFFRACTION

▼

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.

2jj4__assembly_1__model_1

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

Download this curve (.dat)

2jj4__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2jj4__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	40.88 Å
Rg (electron density)	39.83 Å
Total Rg	40.27 Å
Atom count	17096
Residues	2362
Excluded volume	303600 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2jj4__assembly_1__model_1`	dodecameric （12）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	ACETYLGLUTAMATE KINASE
Molecular weight formula_weight	34492.4 kDa
EC 编号 ec_number	2.7.2.8
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	8557

MGSSHHHHHHSSGLVPRGSHMSSEFIEAGAADRVRILSEALPYLQQFAGRTVVVKYGGAAMKQEELKEAVMRDIVFLACVGMRPVVVHGGGPEINAWLGRVGIEPQFHNGLRVTDADTMEVVEMVLVGRVNKDIVSRINTTGGRAVGFCGTDGRLVLARPHDQEGIGFVGEVNSVNSEVIEPLLERGYIPVISSVAADENGQSFNINADTVAGEIAAALNAEKLILLTDTRGILEDPKRPESLIPRLNIPQSRELIAQGIVGGGMIPKVDCCIRSLAQGVRAAHIIDGRIPHALLLEIFTDAGIGTMIVGSGYHEAHQPWQ

Source Source

Source organism organism	SYNECHOCOCCUS ELONGATUS
NCBI taxonomy ID ncbi_taxonomy_id	1140
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	NITROGEN REGULATORY PROTEIN P-II
Molecular weight formula_weight	12409.3 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,E,F

MKKIEAIIRPFKLDEVKIALVNAGIVGMTVSEVRGFGRQKGQTERYRGSEYTVEFLQKLKLEIVVEDAQVDTVIDKIVAAARTGEIGDGKIFVSPVDQTIRIRTGEKNADAI

Source Source

Source organism organism	SYNECHOCOCCUS ELONGATUS
NCBI taxonomy ID ncbi_taxonomy_id	1140
Host organism host_organism	ESCHERICHIA COLI

Entity 3 Entity 3 non-polymer

Description description	N-ACETYL-L-GLUTAMATE
Molecular weight formula_weight	189.2 kDa
Source method src_method	syn
Copy count entity_count	2

▼

6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id	2jj4A00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1160 — Carbamate kinase
Homologous superfamily homologous superfamily	10 — Acetylglutamate kinase-like

Domain ID domain_id	2jj4B00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1160 — Carbamate kinase
Homologous superfamily homologous superfamily	10 — Acetylglutamate kinase-like

Domain ID domain_id	2jj4C00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1160 — Carbamate kinase
Homologous superfamily homologous superfamily	10 — Acetylglutamate kinase-like

Domain ID domain_id	2jj4D00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	120 —

Domain ID domain_id	2jj4E00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	120 —

Domain ID domain_id	2jj4F00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	120 —

▶

Unit-cell length a length_a	106.901 Å
Unit-cell length b length_b	149.539 Å
Unit-cell length c length_c	162.205 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	24

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	3.460 Å
Low-resolution limit resolution_low	50.000 Å
R factor r_factor	0.2360
R_work r_work	0.2330
R_free r_free	0.2940

The complex of PII and acetylglutamate kinase from Synechococcus elongatus PCC7942

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

ACETYLGLUTAMATE KINASE

State in the Current Structure

Other States of the Same Protein in the Database

NITROGEN REGULATORY PROTEIN P-II

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

2jj4__assembly_1__model_1

2jj4__assembly_1__model_1 | I(q)

2jj4__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

7. Citations (1)

The complex of PII and acetylglutamate kinase from Synechococcus elongatus PCC7942

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

ACETYLGLUTAMATE 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

NITROGEN REGULATORY PROTEIN P-II

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

2jj4__assembly_1__model_1

2jj4__assembly_1__model_1 | I(q)

2jj4__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

7. Citations (1)