4AHQ

Crystal Structure of N-acetylneuraminic acid lyase mutant K165C from Staphylococcus aureus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0008747	molecular_function	N-acetylneuraminate lyase activity
A	0016829	molecular_function	lyase activity
A	0019262	biological_process	N-acetylneuraminate catabolic process
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005975	biological_process	carbohydrate metabolic process
B	0008747	molecular_function	N-acetylneuraminate lyase activity
B	0016829	molecular_function	lyase activity
B	0019262	biological_process	N-acetylneuraminate catabolic process
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005975	biological_process	carbohydrate metabolic process
C	0008747	molecular_function	N-acetylneuraminate lyase activity
C	0016829	molecular_function	lyase activity
C	0019262	biological_process	N-acetylneuraminate catabolic process
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005975	biological_process	carbohydrate metabolic process
D	0008747	molecular_function	N-acetylneuraminate lyase activity
D	0016829	molecular_function	lyase activity
D	0019262	biological_process	N-acetylneuraminate catabolic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000255\|HAMAP-Rule:MF_01237

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Schiff-base intermediate with substrate => ECO:0000255\|HAMAP-Rule:MF_01237, ECO:0000269\|PubMed:23418011

site_id	SWS_FT_FI3
Number of Residues	28
Details	BINDING: BINDING => ECO:0000305\|PubMed:27943302, ECO:0007744\|PDB:5KZD