2UYK

Crystal structure of E. coli TdcF with bound serine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005829	cellular_component	cytosol
A	0006566	biological_process	L-threonine metabolic process
A	0016787	molecular_function	hydrolase activity
A	0019239	molecular_function	deaminase activity
A	0042802	molecular_function	identical protein binding
A	0070689	biological_process	obsolete L-threonine catabolic process to propionate
B	0005829	cellular_component	cytosol
B	0006566	biological_process	L-threonine metabolic process
B	0016787	molecular_function	hydrolase activity
B	0019239	molecular_function	deaminase activity
B	0042802	molecular_function	identical protein binding
B	0070689	biological_process	obsolete L-threonine catabolic process to propionate
C	0005829	cellular_component	cytosol
C	0006566	biological_process	L-threonine metabolic process
C	0016787	molecular_function	hydrolase activity
C	0019239	molecular_function	deaminase activity
C	0042802	molecular_function	identical protein binding
C	0070689	biological_process	obsolete L-threonine catabolic process to propionate

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SER C1129

Chain	Residue
A	GLY31
C	HOH2139
A	ILE33
A	GLU120
C	PHE84
C	ARG105
C	SER106
C	CYS107
C	HOH2137
C	HOH2138

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Functional Information from PROSITE/UniProt

site_id	PS01094
Number of Residues	19
Details	UPF0076 Uncharacterized protein family UPF0076 signature. PTRScVqvArLpkdvk...LEI

Chain	Residue	Details
A	PRO103-ILE121

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	Binding site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	3
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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