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1EYB

CRYSTAL STRUCTURE OF APO HUMAN HOMOGENTISATE DIOXYGENASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004411molecular_functionhomogentisate 1,2-dioxygenase activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006520biological_processamino acid metabolic process
A0006559biological_processL-phenylalanine catabolic process
A0006570biological_processtyrosine metabolic process
A0006572biological_processL-tyrosine catabolic process
A0016491molecular_functionoxidoreductase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0070062cellular_componentextracellular exosome
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10876237","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EY2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ey2
ChainResidueDetails
AHIS292
AHIS365

site_idMCSA1
Number of Residues5
DetailsM-CSA 547
ChainResidueDetails
APRO320electrostatic stabiliser, enhance reactivity
ASER363metal ligand
APRO370metal ligand
AGLU401proton acceptor, proton donor
ATRP411metal ligand

246031

PDB entries from 2025-12-10

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