Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9JDB

Structure of chanoclavine synthase from Claviceps fusiformis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004096molecular_functioncatalase activity
A0004601molecular_functionperoxidase activity
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005777cellular_componentperoxisome
A0006979biological_processresponse to oxidative stress
A0009820biological_processalkaloid metabolic process
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0035835biological_processindole alkaloid biosynthetic process
A0042542biological_processresponse to hydrogen peroxide
A0042744biological_processhydrogen peroxide catabolic process
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
B0004096molecular_functioncatalase activity
B0004601molecular_functionperoxidase activity
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005777cellular_componentperoxisome
B0006979biological_processresponse to oxidative stress
B0009820biological_processalkaloid metabolic process
B0016491molecular_functionoxidoreductase activity
B0020037molecular_functionheme binding
B0035835biological_processindole alkaloid biosynthetic process
B0042542biological_processresponse to hydrogen peroxide
B0042744biological_processhydrogen peroxide catabolic process
B0046872molecular_functionmetal ion binding
B0098869biological_processcellular oxidant detoxification
Functional Information from PROSITE/UniProt
site_idPS00437
Number of Residues9
DetailsCATALASE_1 Catalase proximal heme-ligand signature. RLFAYpDAQ
ChainResidueDetails
AARG339-GLN347

site_idPS00438
Number of Residues17
DetailsCATALASE_2 Catalase proximal active site signature. FnRekipERavHarGAG
ChainResidueDetails
APHE42-GLY58

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P15202
ChainResidueDetails
AHIS53
BHIS53

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000250|UniProtKB:P15202
ChainResidueDetails
ATYR343
BTYR343

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon