2yim

The enolisation chemistry of a thioester-dependent racemase: the 1.4 A crystal structure of a complex with a planar reaction intermediate analogue

Method: X-RAY DIFFRACTION

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

PROBABLE ALPHA-METHYLACYL-COA RACEMASE MCR (2-METHYLACYL-COA RACEMASE) (2-ARYLPROPIONYL-COA EPIMERASE )

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 × 2 2-METHYLACETOACETYL COA × 2 PHOSPHATE ION × 1 water × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	GLYCEROL × 3 2-METHYLACETOACETYL COA × 2 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	2yim
Deposition date deposition_date	2011-05-16
Structure title title	The enolisation chemistry of a thioester-dependent racemase: the 1.4 A crystal structure of a complex with a planar reaction intermediate analogue
Keywords keywords	ISOMERASE, METHYL-COA RACEMASE, TRANSITION STATE, MOLECULAR DYNAMICS, QM/MM, OXYANION HOLE; 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.

2yim__assembly_1__model_1

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

Download this curve (.dat)

2yim__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2yim__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	26.03 Å
Rg (electron density)	24.84 Å
Total Rg	25.63 Å
Atom count	5494
Residues	710
Excluded volume	96737 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2yim__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2yim__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 (5)

Entity 1 Entity 1 polymer

Description description	PROBABLE ALPHA-METHYLACYL-COA RACEMASE MCR (2-METHYLACYL-COA RACEMASE) (2-ARYLPROPIONYL-COA EPIMERASE )
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	13495

MAGPLSGLRVVELAGIGPGPHAAMILGDLGADVVRIDRPSSVDGISRDAMLRNRRIVTADLKSDQGLELALKLIAKADVLIEGYRPGVTERLGLGPEECAKVNDRLIYARMTGWGQTGPRSQQAGHDINYISLNGILHAIGRGDERPVPPLNLVGDFGGGSMFLLVGILAALWERQSSGKGQVVDAAMVDGSSVLIQMMWAMRATGMWTDTRGANMLDGGAPYYDTYECADGRYVAVGAIEPQFYAAMLAGLGLDAAELPPQNDRARWPELRALLTEAFASHDRDHWGAVFANSDACVTPVLAFGEVHNEPHIIERNTFYEANGGWQPMPAPRFSRTASSQPRPPAATIDIEAVLTDWDG

Source Source

Source organism organism	MYCOBACTERIUM TUBERCULOSIS
NCBI taxonomy ID ncbi_taxonomy_id	83332
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	5

Entity 3 Entity 3 non-polymer

Description description	2-METHYLACETOACETYL COA
Molecular weight formula_weight	864.6 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1818

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6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d2yima_
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	d2yimb_
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	d2yimc_
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	d2yimd_
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 (8 domains)

Domain ID domain_id	2yimA01
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	2yimA02
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	2yimB01
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	2yimB02
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	2yimC01
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	2yimC02
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	2yimD01
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	2yimD02
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

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Unit-cell length a length_a	181.590 Å
Unit-cell length b length_b	80.170 Å
Unit-cell length c length_c	118.880 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	91.41 °
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	1.410 Å
Low-resolution limit resolution_low	118.840 Å
R factor r_factor	0.1871
R_work r_work	0.1862
R_free r_free	0.2046

The enolisation chemistry of a thioester-dependent racemase: the 1.4 A crystal structure of a complex with a planar reaction intermediate analogue

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

PROBABLE ALPHA-METHYLACYL-COA RACEMASE MCR (2-METHYLACYL-COA RACEMASE) (2-ARYLPROPIONYL-COA EPIMERASE )

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

2yim__assembly_1__model_1

2yim__assembly_1__model_1 | I(q)

2yim__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 (5)

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 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

CATH v4.4 (8 domains)

7. Citations (2)

The enolisation chemistry of a thioester-dependent racemase: the 1.4 A crystal structure of a complex with a planar reaction intermediate analogue

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

PROBABLE ALPHA-METHYLACYL-COA RACEMASE MCR (2-METHYLACYL-COA RACEMASE) (2-ARYLPROPIONYL-COA EPIMERASE )

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

2yim__assembly_1__model_1

2yim__assembly_1__model_1 | I(q)

2yim__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 (5)

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 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

CATH v4.4 (8 domains)

7. Citations (2)