Structure of PDB 2gce Chain A

Receptor sequence

>2gceA (length=354) Species: 1773 (Mycobacterium tuberculosis)

AGPLSGLRVVELAGIGPGPHAAMILGDLGADVVRIDRPISRDAMLRNRRI
VTADLKSDQGLELALKLIAKADVLIEGYRPGVTERLGLGPEECAKVNDRL
IYARMTGWGQTGPRSQQAGHDINYISLNGILHAIGRGDERPVPPLNLVGD
FGGGSMFLLVGILAALWERQSSGKGQVVDAAMVDGSSVLIQMMWAMRATG
MWTDTRGANMLDGGAPYYDTYECADGRYVAVGAIEPQFYAAMLAGLGLDA
AELPPQNDRARWPELRALLTEAFASHDRDHWGAVFANSDACVTPVLAFGE
VHNEPHIIERNTFYEANGGWQPMPAPRFSRTASSQPRPPAATIDIEAVLT
DWDG

3D structure

• PDB: 2gce The Catalysis of the 1,1-Proton Transfer by alpha-Methyl-acyl-CoA Racemase Is Coupled to a Movement of the Fatty Acyl Moiety Over a Hydrophobic, Methionine-rich Surface
• Chain: A
• Resolution: 1.85 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): G17 D127 D156 G219 G220
• Catalytic site (residue number reindexed from 1): G16 D121 D150 G213 G214
• Enzyme Commision number: 5.1.99.4: alpha-methylacyl-CoA racemase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	SFC	A	I16 G17 P18 R38 L61 K62 G83 Y84 R85 V88 R91 G125 H126 Y130 D156	I15 G16 P17 R37 L55 K56 G77 Y78 R79 V82 R85 G119 H120 Y124 D150	MOAD: Kd=24.5uM
BS02	RFC	A	I16 R38 L61 K62 G83 Y84 R85 V88 R91 G125 H126 D127 Y130 D156	I15 R37 L55 K56 G77 Y78 R79 V82 R85 G119 H120 D121 Y124 D150	MOAD: Kd=24.5uM
BS03	RFC	A	L217 Y224 I240	L211 Y218 I234	MOAD: Kd=24.5uM

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0008111 alpha-methylacyl-CoA racemase activity
• GO:0016853 isomerase activity
• GO:0042803 protein homodimerization activity

Biological Process

• GO:0006629 lipid metabolic process
• GO:0006637 acyl-CoA metabolic process

External links

• PDB: RCSB:2gce, PDBe:2gce, PDBj:2gce
• PDBsum: 2gce
• PubMed: 17320106
• UniProt: O06543|AMACR_MYCTU Alpha-methylacyl-CoA racemase (Gene Name=mcr)