2qgq

Crystal structure of TM_1862 from Thermotoga maritima. Northeast Structural Genomics Consortium target VR77

Method: X-RAY DIFFRACTION

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

Protein TM_1862

Thermotoga maritima MSB8

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	3-CYCLOHEXYL-1-PROPYLSULFONIC ACID × 1 water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	3-CYCLOHEXYL-1-PROPYLSULFONIC ACID × 1 water × 1	Consistent with protein count
3	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
4	Protein monomer	Monomer	Protein 1	3-CYCLOHEXYL-1-PROPYLSULFONIC ACID × 1 water × 1	Consistent with protein count
5	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
6	Protein monomer	Monomer	Protein 1	3-CYCLOHEXYL-1-PROPYLSULFONIC ACID × 1 water × 1	Consistent with protein count
7	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
8	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9X2H6_THEMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–296； UniProt 135–430 Author chain B； PDBConstruct 1–296； UniProt 135–430 Author chain C； PDBConstruct 1–296； UniProt 135–430 Author chain D； PDBConstruct 1–296； UniProt 135–430 Author chain E； PDBConstruct 1–296； UniProt 135–430 Author chain F； PDBConstruct 1–296； UniProt 135–430 Author chain G； PDBConstruct 1–296； UniProt 135–430 Author chain H； PDBConstruct 1–296； UniProt 135–430

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	2qgq
Deposition date deposition_date	2007-06-29
Structure title title	Crystal structure of TM_1862 from Thermotoga maritima. Northeast Structural Genomics Consortium target VR77
Keywords keywords	;alpha-beta protein, Structural Genomics, PSI-2, Protein Structure Initiative, Northeast Structural Genomics Consortium, NESG, UNKNOWN FUNCTION ;; STRUCTURAL GENOMICS, UNKNOWN FUNCTION
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.

2qgq__assembly_5__model_1

Assembly 5 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2qgq__assembly_5__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2qgq__assembly_5__model_1 | P(r) · Pending

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

Rg（Guinier）	20.58 Å
Rg (electron density)	19.53 Å
Total Rg	20.46 Å
Atom count	2196
Residues	264
Excluded volume	39519 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2qgq__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2qgq__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2qgq__assembly_3__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`2qgq__assembly_4__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`2qgq__assembly_5__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
6	1	`2qgq__assembly_6__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
7	1	`2qgq__assembly_7__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
8	1	`2qgq__assembly_8__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 (3)

Entity 1 Entity 1 polymer

Description description	Protein TM_1862
Molecular weight formula_weight	35459.6 kDa
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H
Atom count atom_count	19066

EERPYAYVKISDGCDRGCTFCSIPSFKGSLRSRSIEDITREVEDLLKEGKKEIILVAQDTTSYGIDLYRKQALPDLLRRLNSLNGEFWIRVMYLHPDHLTEEIISAMLELDKVVKYFDVPVQHGSDKILKLMGRTKSSEELKKMLSSIRERFPDAVLRTSIIVGFPGETEEDFEELKQFVEEIQFDKLGAFVYSDEEGTVAFNLKEKVDPEMAKRRQEELLLLQAEISNSRLDRFVGKKLKFLVEGKEGKFLVGRTWTEAPEVDGVVFVRGKGKIGDFLEVVIKEHDEYDMWGSVILEHHHHHH

Source Source

Source organism organism	Thermotoga maritima MSB8
NCBI taxonomy ID ncbi_taxonomy_id	243274
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	3-CYCLOHEXYL-1-PROPYLSULFONIC ACID
Molecular weight formula_weight	221.3 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1442

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6. Fold Classification (SCOP + CATH) 16 domains

CATH v4.4 (16 domains)

Domain ID domain_id	2qgqA01
Class class	3 — Alpha Beta
Architecture architecture	80 — Alpha-Beta Horseshoe
Topology topology	30 — pyruvate-formate lyase- activating enzyme
Homologous superfamily homologous superfamily	20 — tm_1862 like domain

Domain ID domain_id	2qgqA02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	2qgqB01
Class class	3 — Alpha Beta
Architecture architecture	80 — Alpha-Beta Horseshoe
Topology topology	30 — pyruvate-formate lyase- activating enzyme
Homologous superfamily homologous superfamily	20 — tm_1862 like domain

Domain ID domain_id	2qgqB02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	2qgqC01
Class class	3 — Alpha Beta
Architecture architecture	80 — Alpha-Beta Horseshoe
Topology topology	30 — pyruvate-formate lyase- activating enzyme
Homologous superfamily homologous superfamily	20 — tm_1862 like domain

Domain ID domain_id	2qgqC02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	2qgqD01
Class class	3 — Alpha Beta
Architecture architecture	80 — Alpha-Beta Horseshoe
Topology topology	30 — pyruvate-formate lyase- activating enzyme
Homologous superfamily homologous superfamily	20 — tm_1862 like domain

Domain ID domain_id	2qgqD02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	2qgqE01
Class class	3 — Alpha Beta
Architecture architecture	80 — Alpha-Beta Horseshoe
Topology topology	30 — pyruvate-formate lyase- activating enzyme
Homologous superfamily homologous superfamily	20 — tm_1862 like domain

Domain ID domain_id	2qgqE02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	2qgqF01
Class class	3 — Alpha Beta
Architecture architecture	80 — Alpha-Beta Horseshoe
Topology topology	30 — pyruvate-formate lyase- activating enzyme
Homologous superfamily homologous superfamily	20 — tm_1862 like domain

Domain ID domain_id	2qgqF02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	2qgqG01
Class class	3 — Alpha Beta
Architecture architecture	80 — Alpha-Beta Horseshoe
Topology topology	30 — pyruvate-formate lyase- activating enzyme
Homologous superfamily homologous superfamily	20 — tm_1862 like domain

Domain ID domain_id	2qgqG02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	2qgqH01
Class class	3 — Alpha Beta
Architecture architecture	80 — Alpha-Beta Horseshoe
Topology topology	30 — pyruvate-formate lyase- activating enzyme
Homologous superfamily homologous superfamily	20 — tm_1862 like domain

Domain ID domain_id	2qgqH02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

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Unit-cell length a length_a	88.620 Å
Unit-cell length b length_b	88.649 Å
Unit-cell length c length_c	96.039 Å
Unit-cell angle α angle_alpha	89.98 °
Unit-cell angle β angle_beta	90.03 °
Unit-cell angle γ angle_gamma	89.91 °
Molecules per unit cell Z z_pdb	8

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

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	39.670 Å
R factor r_factor	0.2120
R_work r_work	0.2120
R_free r_free	0.2510

Crystal structure of TM_1862 from Thermotoga maritima. Northeast Structural Genomics Consortium target VR77

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

Protein TM_1862

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

2qgq__assembly_5__model_1

2qgq__assembly_5__model_1 | I(q)

2qgq__assembly_5__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 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 16 domains

CATH v4.4 (16 domains)

7. Citations (1)

Crystal structure of TM_1862 from Thermotoga maritima. Northeast Structural Genomics Consortium target VR77

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

Protein TM_1862

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

2qgq__assembly_5__model_1

2qgq__assembly_5__model_1 | I(q)

2qgq__assembly_5__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 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 16 domains

CATH v4.4 (16 domains)

7. Citations (1)