1EYB

CRYSTAL STRUCTURE OF APO HUMAN HOMOGENTISATE DIOXYGENASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004411	molecular_function	homogentisate 1,2-dioxygenase activity
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0006520	biological_process	amino acid metabolic process
A	0006559	biological_process	L-phenylalanine catabolic process
A	0006570	biological_process	tyrosine metabolic process
A	0006572	biological_process	L-tyrosine catabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0051213	molecular_function	dioxygenase activity
A	0070062	cellular_component	extracellular exosome

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:10876237, ECO:0007744|PDB:1EY2

Chain	Residue	Details
A	HIS335
A	GLU341
A	HIS371

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS98

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:O09173

Chain	Residue	Details
A	LYS414

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ey2

Chain	Residue	Details
A	HIS292
A	HIS365

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 547

Chain	Residue	Details
A	PRO320	electrostatic stabiliser, enhance reactivity
A	SER363	metal ligand
A	PRO370	metal ligand
A	GLU401	proton acceptor, proton donor
A	TRP411	metal ligand

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