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1SQD

Structural basis for inhibitor selectivity revealed by crystal structures of plant and mammalian 4-hydroxyphenylpyruvate dioxygenases

Functional Information from GO Data
ChainGOidnamespacecontents
A0003868molecular_function4-hydroxyphenylpyruvate dioxygenase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0006559biological_processL-phenylalanine catabolic process
A0006572biological_processtyrosine catabolic process
A0009072biological_processaromatic amino acid metabolic process
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 Residues6
DetailsBINDING SITE FOR RESIDUE FE A 500
ChainResidue
AHIS205
AHIS287
AGLU373
AHOH1001
AHOH1011
AHOH1012

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15301540
ChainResidueDetails
AHIS205
AHIS287
AGLU373

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PDB entries from 2024-07-24

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