Structure of PDB 1xfc Chain A

Receptor sequence
>1xfcA (length=366) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
LAEAMVDLGAIEHNVRVLREHAGHAQLMAVVKADGYGHGATRVAQTALGA
GAAELGVATVDEALALRADGITAPVLAWLHPPGIDFGPALLADVQVAVSS
LRQLDELLHAVRRTGRTATVTVKVDTGLNRNGVGPAQFPAMLTALRQAMA
EDAVRLRGLMSHMPDDSINDVQAQRFTAFLAQAREQGVRFEVAHLSNSSA
TMARPDLTFDLVRPGIAVYGLSPVPALGDMGLVPAMTVKCAVALVKSIRA
GEGVSYGHTWIAPRDTNLALLPIGYADGVFRSLGGRLEVLINGRRCPGVG
RICMDQFMVDLGPGPLDVAEGDEAILFGPGIRGEPTAQDWADLVGTIHYE
VVTSPRGRITRTYREA
3D structure
PDB1xfc The 1.9 A crystal structure of alanine racemase from Mycobacterium tuberculosis contains a conserved entryway into the active site.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K42 R140 H172 R228 C318 D320
Catalytic site (residue number reindexed from 1) K32 R130 H162 R213 C303 D305
Enzyme Commision number 5.1.1.1: alanine 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 PLP A K42 Y46 W88 H172 S213 R228 G230 I231 Y364 K32 Y36 W78 H162 S198 R213 G215 I216 Y349
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005515 protein binding
GO:0008784 alanine racemase activity
GO:0016853 isomerase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006522 alanine metabolic process
GO:0009252 peptidoglycan biosynthetic process
GO:0030632 D-alanine biosynthetic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1xfc, PDBe:1xfc, PDBj:1xfc
PDBsum1xfc
PubMed15683232
UniProtP9WQA9|ALR_MYCTU Alanine racemase (Gene Name=alr)

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