1x74

Alpha-methylacyl-CoA racemase from Mycobacterium tuberculosis- mutational and structural characterization of the fold and active site

Method: X-RAY DIFFRACTION

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

2-methylacyl-CoA racemase

Mycobacterium tuberculosis

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	GLYCEROL × 7 water × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	GLYCEROL × 8 PHOSPHATE ION × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	O06543_MYCTU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–360； UniProt 1–360 Author chain B； PDBConstruct 1–360； UniProt 1–360 Author chain C； PDBConstruct 1–360； UniProt 1–360 Author chain D； PDBConstruct 1–360； UniProt 1–360

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	1x74
Deposition date deposition_date	2004-08-13
Structure title title	Alpha-methylacyl-CoA racemase from Mycobacterium tuberculosis- mutational and structural characterization of the fold and active site
Keywords keywords	Alpha-methylacyl-CoA racemase, racemase, CoA transferase, Coenzyme A, ISOMERASE; ISOMERASE
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.

1x74__assembly_2__model_1

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

Download this curve (.dat)

1x74__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1x74__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	25.96 Å
Rg (electron density)	24.77 Å
Total Rg	25.58 Å
Atom count	5411
Residues	708
Excluded volume	95571 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1x74__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1x74__assembly_2__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 (4)

Entity 1 Entity 1 polymer

Description description	2-methylacyl-CoA racemase
Molecular weight formula_weight	38722.8 kDa
EC 编号 ec_number	5.1.99.4
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	12445

MAGPLSGLRVVELAGIGPGPHAAMILGDLGADVVRIDRPSSVDGISRDAMLRNRRIVTADLKSDQGLELALKLIAKADVLIEGYRPGVTERLGLGPEECAKVNDRLIYARMTGWGQTGPRSQQAGHDINYISLNGILHAIGRGDERPVPPLNLVGDFGGGSMFLLVGILAALWERQSSGKGQVVDAAMVDGSSVLIQMMWAMRATGMWTDTRGANMLDGGAPYYDTYECADGRYVAVGAIEPQFYAAMLAGLGLDAAELPPQNDRARWPELRALLTEAFASHDRDHWGAVFANSDACVTPVLAFGEVHNEPHIIERNTFYEANGGWQPMPAPRFSRTASSQPRPPAATIDIEAVLTDWDG

Source Source

Source organism organism	Mycobacterium tuberculosis
NCBI taxonomy ID ncbi_taxonomy_id	1773
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	15

Entity 3 Entity 3 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1458

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6. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1x74a1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.123 — CoA-transferase family III (CaiB/BaiF)
Superfamily Superfamily superfamily	c.123.1 — CoA-transferase family III (CaiB/BaiF)
Family Family family	c.123.1.1 — CoA-transferase family III (CaiB/BaiF)

Domain ID domain_id	d1x74b_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.123 — CoA-transferase family III (CaiB/BaiF)
Superfamily Superfamily superfamily	c.123.1 — CoA-transferase family III (CaiB/BaiF)
Family Family family	c.123.1.1 — CoA-transferase family III (CaiB/BaiF)

Domain ID domain_id	d1x74c_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.123 — CoA-transferase family III (CaiB/BaiF)
Superfamily Superfamily superfamily	c.123.1 — CoA-transferase family III (CaiB/BaiF)
Family Family family	c.123.1.1 — CoA-transferase family III (CaiB/BaiF)

Domain ID domain_id	d1x74d_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.123 — CoA-transferase family III (CaiB/BaiF)
Superfamily Superfamily superfamily	c.123.1 — CoA-transferase family III (CaiB/BaiF)
Family Family family	c.123.1.1 — CoA-transferase family III (CaiB/BaiF)

CATH v4.4 (20 domains)

Domain ID domain_id	1x74A01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10540 — Crotonobetainyl-coa:carnitine coa-transferase; domain 1

Domain ID domain_id	1x74A02
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	140 — Helix Hairpins
Homologous superfamily homologous superfamily	330 —

Domain ID domain_id	1x74A03
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	260 —

Domain ID domain_id	1x74A04
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1540 — formyl-coa transferase, domain 3
Homologous superfamily homologous superfamily	10 — formyl-coa transferase, domain 3

Domain ID domain_id	1x74A05
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	60 — Wheat Germ Agglutinin (Isolectin 2); domain 1
Homologous superfamily homologous superfamily	110 —

Domain ID domain_id	1x74B01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10540 — Crotonobetainyl-coa:carnitine coa-transferase; domain 1

Domain ID domain_id	1x74B02
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	140 — Helix Hairpins
Homologous superfamily homologous superfamily	330 —

Domain ID domain_id	1x74B03
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	260 —

Domain ID domain_id	1x74B04
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1540 — formyl-coa transferase, domain 3
Homologous superfamily homologous superfamily	10 — formyl-coa transferase, domain 3

Domain ID domain_id	1x74B05
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	60 — Wheat Germ Agglutinin (Isolectin 2); domain 1
Homologous superfamily homologous superfamily	110 —

Domain ID domain_id	1x74C01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10540 — Crotonobetainyl-coa:carnitine coa-transferase; domain 1

Domain ID domain_id	1x74C02
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	140 — Helix Hairpins
Homologous superfamily homologous superfamily	330 —

Domain ID domain_id	1x74C03
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	260 —

Domain ID domain_id	1x74C04
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1540 — formyl-coa transferase, domain 3
Homologous superfamily homologous superfamily	10 — formyl-coa transferase, domain 3

Domain ID domain_id	1x74C05
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	60 — Wheat Germ Agglutinin (Isolectin 2); domain 1
Homologous superfamily homologous superfamily	110 —

Domain ID domain_id	1x74D01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10540 — Crotonobetainyl-coa:carnitine coa-transferase; domain 1

Domain ID domain_id	1x74D02
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	140 — Helix Hairpins
Homologous superfamily homologous superfamily	330 —

Domain ID domain_id	1x74D03
Class class	6 — Special
Architecture architecture	10 — Helix non-globular
Topology topology	250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	260 —

Domain ID domain_id	1x74D04
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1540 — formyl-coa transferase, domain 3
Homologous superfamily homologous superfamily	10 — formyl-coa transferase, domain 3

Domain ID domain_id	1x74D05
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	60 — Wheat Germ Agglutinin (Isolectin 2); domain 1
Homologous superfamily homologous superfamily	110 —

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Unit-cell length a length_a	180.073 Å
Unit-cell length b length_b	79.779 Å
Unit-cell length c length_c	117.619 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	92.04 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	16

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	1.790 Å
Low-resolution limit resolution_low	19.960 Å
R factor r_factor	0.1621
R_work r_work	0.1605
R_free r_free	0.1933

Alpha-methylacyl-CoA racemase from Mycobacterium tuberculosis- mutational and structural characterization of the fold and active site

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

2-methylacyl-CoA racemase

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

1x74__assembly_2__model_1

1x74__assembly_2__model_1 | I(q)

1x74__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 (4)

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 water

6. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (4 domains)

CATH v4.4 (20 domains)

7. Citations (1)

Alpha-methylacyl-CoA racemase from Mycobacterium tuberculosis- mutational and structural characterization of the fold and active site

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

2-methylacyl-CoA racemase

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

1x74__assembly_2__model_1

1x74__assembly_2__model_1 | I(q)

1x74__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 (4)

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 water

6. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (4 domains)

CATH v4.4 (20 domains)

7. Citations (1)