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6M6D

Structure of HPPD complexed with a synthesized inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0003868molecular_function4-hydroxyphenylpyruvate dioxygenase activity
A0005506molecular_functioniron ion binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006559biological_processL-phenylalanine catabolic process
A0006572biological_processL-tyrosine catabolic process
A0009072biological_processaromatic amino acid metabolic process
A0009507cellular_componentchloroplast
A0010189biological_processvitamin E biosynthetic process
A0010236biological_processplastoquinone biosynthetic process
A0016117biological_processcarotenoid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016701molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CO A 501
ChainResidue
AHIS226
AHIS308
AGLU394
ANJX502
AHOH644

site_idAC2
Number of Residues15
Detailsbinding site for residue NJX A 502
ChainResidue
AARG290
AHIS308
APHE381
AGLU394
APHE419
AGLY420
AASN423
APHE424
ALEU427
ACO501
AHOH644
AHIS226
ASER267
APRO280
AASN282

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15301540
ChainResidueDetails
AHIS226
AHIS308
AGLU394

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PDB entries from 2025-06-18

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