Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7PXX

The crystal structure of Leishmania major Pteridine Reductase 1 in complex with substrate folic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0004155molecular_function6,7-dihydropteridine reductase activity
A0005829cellular_componentcytosol
A0006729biological_processtetrahydrobiopterin biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0031427biological_processresponse to methotrexate
A0047040molecular_functionpteridine reductase activity
B0004155molecular_function6,7-dihydropteridine reductase activity
B0005829cellular_componentcytosol
B0006729biological_processtetrahydrobiopterin biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0031427biological_processresponse to methotrexate
B0047040molecular_functionpteridine reductase activity
C0004155molecular_function6,7-dihydropteridine reductase activity
C0005829cellular_componentcytosol
C0006729biological_processtetrahydrobiopterin biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0031427biological_processresponse to methotrexate
C0047040molecular_functionpteridine reductase activity
D0004155molecular_function6,7-dihydropteridine reductase activity
D0005829cellular_componentcytosol
D0006729biological_processtetrahydrobiopterin biosynthetic process
D0016491molecular_functionoxidoreductase activity
D0031427biological_processresponse to methotrexate
D0047040molecular_functionpteridine reductase activity
Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. DamtnqpllgYtiYTMAKGALeGLTrSAA
ChainResidueDetails
BASP181-ALA209
AASP181-ALA209

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
BTYR194
CTYR194
DTYR194

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BARG17
CARG17
DARG17

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11373620
ChainResidueDetails
BSER175
CSER175
DSER175

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon