Structure of PDB 2gd2 Chain A

Receptor sequence
>2gd2A (length=354) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
AGPLSGLRVVELAGIGPGPHAAMILGDLGADVVRIDRPISRDAMLRNRRI
VTADLKSDQGLELALKLIAKADVLIEGYRPGVTERLGLGPEECAKVNDRL
IYARMTGWGQTGPRSQQAGHDINYISLNGILHAIGRGDERPVPPLNLVGD
FGGGSMFLLVGILAALWERQSSGKGQVVDAAMVDGSSVLIQMMWAMRATG
MWTDTRGANMLDGGAPYYDTYECADGRYVAVGAIEPQFYAAMLAGLGLDA
AELPPQNDRARWPELRALLTEAFASHDRDHWGAVFANSDACVTPVLAFGE
VHNEPHIIERNTFYEANGGWQPMPAPRFSRTASSQPRPPAATIDIEAVLT
DWDG
3D structure
PDB2gd2 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
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 CAA A I16 R38 A59 L61 K62 G83 Y84 R85 V88 R91 L92 A124 G125 H126 Y130 D156 I15 R37 A53 L55 K56 G77 Y78 R79 V82 R85 L86 A118 G119 H120 Y124 D150
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

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Molecular Function
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Biological Process
External links
PDB RCSB:2gd2, PDBe:2gd2, PDBj:2gd2
PDBsum2gd2
PubMed17320106
UniProtO06543|AMACR_MYCTU Alpha-methylacyl-CoA racemase (Gene Name=mcr)

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