1UOU

Crystal structure of human thymidine phosphorylase in complex with a small molecule inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000002	biological_process	mitochondrial genome maintenance
A	0001525	biological_process	angiogenesis
A	0004645	molecular_function	1,4-alpha-oligoglucan phosphorylase activity
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0006206	biological_process	pyrimidine nucleobase metabolic process
A	0006213	biological_process	pyrimidine nucleoside metabolic process
A	0006935	biological_process	chemotaxis
A	0007165	biological_process	signal transduction
A	0008083	molecular_function	growth factor activity
A	0009032	molecular_function	thymidine phosphorylase activity
A	0016154	molecular_function	pyrimidine-nucleoside phosphorylase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0016763	molecular_function	pentosyltransferase activity
A	0030154	biological_process	cell differentiation
A	0031641	biological_process	regulation of myelination
A	0042803	molecular_function	protein homodimerization activity
A	0046074	biological_process	dTMP catabolic process
A	0051969	biological_process	regulation of transmission of nerve impulse
A	1905333	biological_process	regulation of gastric motility

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CMU A1481

Functional Information from PROSITE/UniProt

site_id	PS00647
Number of Residues	16
Details	THYMID_PHOSPHORYLASE Thymidine and pyrimidine-nucleoside phosphorylases signature. SGRGLghTGGTlDkLE

Chain	Residue	Details
A	SER144-GLU159

Functional Information from SwissProt/UniProt

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1azy

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1azy