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3LG0

Structure of Plasmodium falciparum ornithine delta-aminotransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004587molecular_functionornithine aminotransferase activity
A0005737cellular_componentcytoplasm
A0006591biological_processornithine metabolic process
A0008483molecular_functiontransaminase activity
A0010121biological_processarginine catabolic process to proline via ornithine
A0019544biological_processarginine catabolic process to glutamate
A0030170molecular_functionpyridoxal phosphate binding
A0042802molecular_functionidentical protein binding
A0055129biological_processL-proline biosynthetic process
B0004587molecular_functionornithine aminotransferase activity
B0005737cellular_componentcytoplasm
B0006591biological_processornithine metabolic process
B0008483molecular_functiontransaminase activity
B0010121biological_processarginine catabolic process to proline via ornithine
B0019544biological_processarginine catabolic process to glutamate
B0030170molecular_functionpyridoxal phosphate binding
B0042802molecular_functionidentical protein binding
B0055129biological_processL-proline biosynthetic process
C0004587molecular_functionornithine aminotransferase activity
C0005737cellular_componentcytoplasm
C0006591biological_processornithine metabolic process
C0008483molecular_functiontransaminase activity
C0010121biological_processarginine catabolic process to proline via ornithine
C0019544biological_processarginine catabolic process to glutamate
C0030170molecular_functionpyridoxal phosphate binding
C0042802molecular_functionidentical protein binding
C0055129biological_processL-proline biosynthetic process
D0004587molecular_functionornithine aminotransferase activity
D0005737cellular_componentcytoplasm
D0006591biological_processornithine metabolic process
D0008483molecular_functiontransaminase activity
D0010121biological_processarginine catabolic process to proline via ornithine
D0019544biological_processarginine catabolic process to glutamate
D0030170molecular_functionpyridoxal phosphate binding
D0042802molecular_functionidentical protein binding
D0055129biological_processL-proline biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00600
Number of Residues38
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. FVaDEVqt.GLgRtGkllcthhygvkp....DVIllGKalsGG
ChainResidueDetails
APHE230-GLY267

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250|UniProtKB:P04181
ChainResidueDetails
ALYS262
BLYS262
CLYS262
DLYS262

226707

PDB entries from 2024-10-30

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