SAXSdb — 2iop

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

Chaperone protein htpG

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	ADENOSINE-5'-DIPHOSPHATE × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	ADENOSINE-5'-DIPHOSPHATE × 2	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 4	ADENOSINE-5'-DIPHOSPHATE × 4	Consistent with protein count
4	Protein homooligomer	Homooligomer	Protein 2	ADENOSINE-5'-DIPHOSPHATE × 2	Consistent with protein count
5	Protein homooligomer	Homooligomer	Protein 2	ADENOSINE-5'-DIPHOSPHATE × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	HTPG_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–624； UniProt 1–624 Author chain B； PDBConstruct 1–624； UniProt 1–624 Author chain C； PDBConstruct 1–624； UniProt 1–624 Author chain D； PDBConstruct 1–624； UniProt 1–624

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	2iop
Deposition date deposition_date	2006-10-10
Structure title title	Crystal Structure of Full-length HtpG, the Escherichia coli Hsp90, Bound to ADP
Keywords keywords	Heat Shock Protein, Chaperone, Hsp90; CHAPERONE
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.

2iop__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2iop__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2iop__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	43.47 Å
Rg (electron density)	43.18 Å
Total Rg	43.41 Å
Atom count	9580
Residues	1210
Excluded volume	169300 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2iop__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2iop__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2iop__assembly_3__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`2iop__assembly_4__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`2iop__assembly_5__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	Chaperone protein htpG
Molecular weight formula_weight	71519.4 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	19391

MKGQETRGFQSEVKQLLHLMIHSLYSNKEIFLRELISNASDAADKLRFRALSNPDLYEGDGELRVRVSFDKDKRTLTISDNGVGMTRDEVIDHLGTIAKSGTKSFLESLGSDQAKDSQLIGQFGVGFYSAFIVADKVTVRTRAAGEKPENGVFWESAGEGEYTVADITKEDRGTEITLHLREGEDEFLDDWRVRSIISKYSDHIALPVEIEKREEKDGETVISWEKINKAQALWTRNKSEITDEEYKEFYKHIAHDFNDPLTWSHNRVEGKQEYTSLLYIPSQAPWDMWNRDHKHGLKLYVQRVFIMDDAEQFMPNYLRFVRGLIDSSDLPLNVSREILQDSTVTRNLRNALTKRVLQMLEKLAKDDAEKYQTFWQQFGLVLKEGPAEDFANQEAIAKLLRFASTHTDSSAQTVSLEDYVSRMKEGQEKIYYITADSYAAAKSSPHLELLRKKGIEVLLLSDRIDEWMMNYLTEFDGKPFQSVSKVDESLEKLADEVDESAKEAEKALTPFIDRVKALLGERVKDVRLTHRLTDTPAIVSTDADEMSTQMAKLFAAAGQKVPEVKYIFELNPDHVLVKRAADTEDEAKFSEWVELLLDQALLAERGTLEDPNLFIRRMNQLLVS

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 non-polymer

Description description	ADENOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	427.2 kDa
Source method src_method	syn
Copy count entity_count	4

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6. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id	2iopA01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	565 — Heat Shock Protein 90
Homologous superfamily homologous superfamily	10 — Histidine kinase-like ATPase, C-terminal domain

Domain ID domain_id	2iopA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	230 — Ribosomal Protein S5; domain 2
Homologous superfamily homologous superfamily	80 —

Domain ID domain_id	2iopB01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	565 — Heat Shock Protein 90
Homologous superfamily homologous superfamily	10 — Histidine kinase-like ATPase, C-terminal domain

Domain ID domain_id	2iopB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	230 — Ribosomal Protein S5; domain 2
Homologous superfamily homologous superfamily	80 —

Domain ID domain_id	2iopC01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	565 — Heat Shock Protein 90
Homologous superfamily homologous superfamily	10 — Histidine kinase-like ATPase, C-terminal domain

Domain ID domain_id	2iopC02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	230 — Ribosomal Protein S5; domain 2
Homologous superfamily homologous superfamily	80 —

Domain ID domain_id	2iopD01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	565 — Heat Shock Protein 90
Homologous superfamily homologous superfamily	10 — Histidine kinase-like ATPase, C-terminal domain

Domain ID domain_id	2iopD02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	230 — Ribosomal Protein S5; domain 2
Homologous superfamily homologous superfamily	80 —

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Unit-cell length a length_a	78.618 Å
Unit-cell length b length_b	145.060 Å
Unit-cell length c length_c	165.352 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	92.43 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	3.550 Å
Low-resolution limit resolution_low	46.600 Å
R factor r_factor	—
R_work r_work	0.3170
R_free r_free	0.3570

Crystal Structure of Full-length HtpG, the Escherichia coli Hsp90, Bound to ADP

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

Chaperone protein htpG

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

2iop__assembly_2__model_1

2iop__assembly_2__model_1 | I(q)

2iop__assembly_2__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 non-polymer

6. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

7. Citations (1)

Crystal Structure of Full-length HtpG, the Escherichia coli Hsp90, Bound to ADP

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

Chaperone protein htpG

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

2iop__assembly_2__model_1

2iop__assembly_2__model_1 | I(q)

2iop__assembly_2__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 non-polymer

6. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

7. Citations (1)