3LG0

Structure of Plasmodium falciparum ornithine delta-aminotransferase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004587	molecular_function	L-ornithine transaminase activity
A	0005737	cellular_component	cytoplasm
A	0006591	biological_process	ornithine metabolic process
A	0030170	molecular_function	pyridoxal phosphate binding
A	0055129	biological_process	L-proline biosynthetic process
B	0004587	molecular_function	L-ornithine transaminase activity
B	0005737	cellular_component	cytoplasm
B	0006591	biological_process	ornithine metabolic process
B	0030170	molecular_function	pyridoxal phosphate binding
B	0055129	biological_process	L-proline biosynthetic process
C	0004587	molecular_function	L-ornithine transaminase activity
C	0005737	cellular_component	cytoplasm
C	0006591	biological_process	ornithine metabolic process
C	0030170	molecular_function	pyridoxal phosphate binding
C	0055129	biological_process	L-proline biosynthetic process
D	0004587	molecular_function	L-ornithine transaminase activity
D	0005737	cellular_component	cytoplasm
D	0006591	biological_process	ornithine metabolic process
D	0030170	molecular_function	pyridoxal phosphate binding
D	0055129	biological_process	L-proline biosynthetic process

Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	38
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. FVaDEVqt.GLgRtGkllcthhygvkp....DVIllGKalsGG

Chain	Residue	Details
A	PHE230-GLY267

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"UniProtKB","id":"P04181","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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