Structure of PDB 2gce Chain D

Receptor sequence

>2gceD (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: D
• 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	RFC	D	Y224 I240	Y218 I234	MOAD: Kd=24.5uM
BS02	SFC	D	G17 R38 L61 K62 Y84 R85 V88 R91 L92 T112 A124 G125 H126 D127 Y130 N152 D156 M188	G16 R37 L55 K56 Y78 R79 V82 R85 L86 T106 A118 G119 H120 D121 Y124 N146 D150 M182	MOAD: Kd=24.5uM
BS03	RFC	D	I16 R38 L61 K62 Y84 R85 V88 R91 L92 T112 A124 G125 H126 D127 Y130 D156	I15 R37 L55 K56 Y78 R79 V82 R85 L86 T106 A118 G119 H120 D121 Y124 D150	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)