7PEK

Crystal structure of Triosephosphate Isomerase C216A mutant from Schizosaccharomyces pombe (SpTIM C216A)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004807	molecular_function	triose-phosphate isomerase activity
A	0005634	cellular_component	nucleus
A	0005829	cellular_component	cytosol
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0016853	molecular_function	isomerase activity
A	0019563	biological_process	glycerol catabolic process
A	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
A	0061621	biological_process	canonical glycolysis
B	0004807	molecular_function	triose-phosphate isomerase activity
B	0005634	cellular_component	nucleus
B	0005829	cellular_component	cytosol
B	0006094	biological_process	gluconeogenesis
B	0006096	biological_process	glycolytic process
B	0016853	molecular_function	isomerase activity
B	0019563	biological_process	glycerol catabolic process
B	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
B	0061621	biological_process	canonical glycolysis
C	0004807	molecular_function	triose-phosphate isomerase activity
C	0005634	cellular_component	nucleus
C	0005829	cellular_component	cytosol
C	0006094	biological_process	gluconeogenesis
C	0006096	biological_process	glycolytic process
C	0016853	molecular_function	isomerase activity
C	0019563	biological_process	glycerol catabolic process
C	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
C	0061621	biological_process	canonical glycolysis
D	0004807	molecular_function	triose-phosphate isomerase activity
D	0005634	cellular_component	nucleus
D	0005829	cellular_component	cytosol
D	0006094	biological_process	gluconeogenesis
D	0006096	biological_process	glycolytic process
D	0016853	molecular_function	isomerase activity
D	0019563	biological_process	glycerol catabolic process
D	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
D	0061621	biological_process	canonical glycolysis

Functional Information from PROSITE/UniProt

site_id	PS00171
Number of Residues	11
Details	TIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG

Chain	Residue	Details
A	ALA162-GLY172

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Electrophile => ECO:0000250

Chain	Residue	Details
A	HIS95
B	HIS95
C	HIS95
D	HIS95

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site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000250

Chain	Residue	Details
A	PRO165
B	PRO165
C	PRO165
D	PRO165

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site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	ASN10
A	LYS12
B	ASN10
B	LYS12
C	ASN10
C	LYS12
D	ASN10
D	LYS12

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site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:18257517

Chain	Residue	Details
A	SER105
A	VAL199
B	SER105
B	VAL199
C	SER105
C	VAL199
D	SER105
D	VAL199

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