Structure of PDB 2yim Chain D

Receptor sequence
>2yimD (length=355) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
AGPLSGLRVVELAGIGPGPHAAMILGDLGADVVRIDRPSISRDAMLRNRR
IVTADLKSDQGLELALKLIAKADVLIEGYRPGVTERLGLGPEECAKVNDR
LIYARMTGWGQTGPRSQQAGHDINYISLNGILHAIGRGDERPVPPLNLVG
DFGGGSMFLLVGILAALWERQSSGKGQVVDAAMVDGSSVLIQMMWAMRAT
GMWTDTRGANMLDGGAPYYDTYECADGRYVAVGAIEPQFYAAMLAGLGLD
AAELPPQNDRARWPELRALLTEAFASHDRDHWGAVFANSDACVTPVLAFG
EVHNEPHIIERNTFYEANGGWQPMPAPRFSRTASSQPRPPAATIDIEAVL
TDWDG
3D structure
PDB2yim The Enolization Chemistry of a Thioester-Dependent Racemase: The 1.4 A Crystal Structure of a Reaction Intermediate Complex Characterized by Detailed Qm/Mm Calculations.
ChainD
Resolution1.41 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 D122 D151 G214 G215
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 MC4 D I16 R38 A59 L61 K62 G83 Y84 R85 V88 R91 L92 A124 G125 H126 Y130 D156 I15 R37 A54 L56 K57 G78 Y79 R80 V83 R86 L87 A119 G120 H121 Y125 D151 MOAD: Kd=120uM
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:2yim, PDBe:2yim, PDBj:2yim
PDBsum2yim
PubMed22360758
UniProtO06543|AMACR_MYCTU Alpha-methylacyl-CoA racemase (Gene Name=mcr)

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