SAXSdb — 3pcs

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

EspG

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Serine/threonine-protein kinase PAK 2 × 1 （Q13177）	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Serine/threonine-protein kinase PAK 2 × 1 （Q13177）	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	Serine/threonine-protein kinase PAK 2 × 1 （Q13177）	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 2	Serine/threonine-protein kinase PAK 2 × 1 （Q13177）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q7DB50_ECO57
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–357； UniProt 42–398 Author chain B； PDBConstruct 1–357； UniProt 42–398 Author chain C； PDBConstruct 1–357； UniProt 42–398 Author chain D； PDBConstruct 1–357； UniProt 42–398

Serine/threonine-protein kinase PAK 2

Homo sapiens

UniProt Q13177

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	EspG × 1 （Q7DB50）	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	EspG × 1 （Q7DB50）	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	EspG × 1 （Q7DB50）	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 2	EspG × 1 （Q7DB50）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PAK2_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain E； PDBConstruct 1–16； UniProt 121–136 Author chain F； PDBConstruct 1–16； UniProt 121–136 Author chain G； PDBConstruct 1–16； UniProt 121–136 Author chain H； PDBConstruct 1–16； UniProt 121–136

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	3pcs
Deposition date deposition_date	2010-10-21
Structure title title	Structure of EspG-PAK2 autoinhibitory Ialpha3 helix complex
Keywords keywords	BACTERIAL EFFECTOR, KINASE, AUTOINHIBITORY IALPHA3 HELIX, PROTEIN TRANSPORT-TRANSFERASE complex; PROTEIN TRANSPORT/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.

3pcs__assembly_4__model_1

Assembly 4 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

3pcs__assembly_4__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3pcs__assembly_4__model_1 | P(r) · Pending

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

Rg（Guinier）	21.53 Å
Rg (electron density)	20.30 Å
Total Rg	21.23 Å
Atom count	2808
Residues	361
Excluded volume	49659 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3pcs__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3pcs__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`3pcs__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`3pcs__assembly_4__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 (2)

Entity 1 Entity 1 polymer

Description description	EspG
Molecular weight formula_weight	39611.4 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	11254

KKSWDEMSCAEKLFKVLSFGLWNPTYSRSERQSFQELLTVLEPVYPLPNELGRVSARFSDGSSLRISVTNSELVEAEIRTANNEKITVLLESNEQNRLLQSLPIDRHMPYIQVHRALSEMDLTDTTSMRNLLGFTSKLSTTLIPHNAQTDPLSGPTPFSSIFMDTCRGLGNAKLSLNGVDIPANAQKLLRDALGLKDTHSSPTRNVIDHGISRHDAEQIARESSGSDKQKAEVVEFLCHPEAATAICSAFYQSFNVPALTLTHERISKASEYNAERSLDTPNACINISISQSSDGNIYVTSHTGVLIMAPEDRPNEMGMLTNRTSYEVPQGVKCIIDEMVSALQPRYAASETYLQNT

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	83334
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Serine/threonine-protein kinase PAK 2
Molecular weight formula_weight	1842.1 kDa
EC 编号 ec_number	2.7.11.1
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

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

QAVLDVLKFYDSNTVK

Source Source

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

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6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id	3pcsA01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	460 — EspG protein, N-terminal domain

Domain ID domain_id	3pcsB01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	460 — EspG protein, N-terminal domain

Domain ID domain_id	3pcsC01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	460 — EspG protein, N-terminal domain

Domain ID domain_id	3pcsD01
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	460 — EspG protein, N-terminal domain

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Unit-cell length a length_a	86.717 Å
Unit-cell length b length_b	104.603 Å
Unit-cell length c length_c	191.994 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	16

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

Resolution resolution	2.860 Å
Low-resolution limit resolution_low	40.500 Å
R factor r_factor	0.1950
R_work r_work	0.1910
R_free r_free	0.2810

Structure of EspG-PAK2 autoinhibitory Ialpha3 helix complex

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

EspG

State in the Current Structure

Other States of the Same Protein in the Database

Serine/threonine-protein kinase PAK 2

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

3pcs__assembly_4__model_1

3pcs__assembly_4__model_1 | I(q)

3pcs__assembly_4__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

7. Citations (1)

Structure of EspG-PAK2 autoinhibitory Ialpha3 helix complex

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

EspG

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Serine/threonine-protein kinase PAK 2

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

3pcs__assembly_4__model_1

3pcs__assembly_4__model_1 | I(q)

3pcs__assembly_4__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

7. Citations (1)