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

8A3N

Geissoschizine synthase from Catharanthus roseus - binary complex with NADP+

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0009753biological_processresponse to jasmonic acid
A0009809biological_processlignin biosynthetic process
A0010272biological_processresponse to silver ion
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0035834biological_processindole alkaloid metabolic process
A0045551molecular_functioncinnamyl-alcohol dehydrogenase activity
A0046872molecular_functionmetal ion binding
A0047920molecular_functiongeissoschizine dehydrogenase activity
B0008270molecular_functionzinc ion binding
B0009753biological_processresponse to jasmonic acid
B0009809biological_processlignin biosynthetic process
B0010272biological_processresponse to silver ion
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0035834biological_processindole alkaloid metabolic process
B0045551molecular_functioncinnamyl-alcohol dehydrogenase activity
B0046872molecular_functionmetal ion binding
B0047920molecular_functiongeissoschizine dehydrogenase activity
Functional Information from PROSITE/UniProt
site_idPS00059
Number of Residues15
DetailsADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEtAGEvvevGskV
ChainResidueDetails
AGLY72-VAL86

site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CMVGSCGQC
ChainResidueDetails
ACYS99-CYS107

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P06525
ChainResidueDetails
ACYS51
BHIS73
BCYS104
BCYS107
BCYS110
BCYS118
BCYS168
BGLY193
AHIS73
ACYS104
ACYS107
ACYS110
ACYS118
ACYS168
AGLY193
BCYS51

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00327
ChainResidueDetails
AVAL280
BVAL280

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon