1DHN

1.65 ANGSTROM RESOLUTION STRUCTURE OF 7,8-DIHYDRONEOPTERIN ALDOLASE FROM STAPHYLOCOCCUS AUREUS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004150	molecular_function	dihydroneopterin aldolase activity
A	0005737	cellular_component	cytoplasm
A	0006760	biological_process	folic acid-containing compound metabolic process
A	0016829	molecular_function	lyase activity
A	0016853	molecular_function	isomerase activity
A	0046654	biological_process	tetrahydrofolate biosynthetic process
A	0046656	biological_process	folic acid biosynthetic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"17331536","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9586996","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17331536","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9586996","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2NM2","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

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

Chain	Residue	Details
A	GLU22
A	LYS100

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site_id	MCSA1
Number of Residues	2
Details	M-CSA 664

Chain	Residue	Details
A	GLU22	electrostatic stabiliser
A	LYS100	proton acceptor, proton donor

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