2NM2

Crystal structure of dihydroneopterin aldolase from S. aureus in complex with (1S,2R)-neopterin at 1.50 Angstrom resolution

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
B	0004150	molecular_function	dihydroneopterin aldolase activity
B	0005737	cellular_component	cytoplasm
B	0006760	biological_process	folic acid-containing compound metabolic process
B	0016829	molecular_function	lyase activity
B	0016853	molecular_function	isomerase activity
B	0046654	biological_process	tetrahydrofolate biosynthetic process
B	0046656	biological_process	folic acid biosynthetic process
C	0004150	molecular_function	dihydroneopterin aldolase activity
C	0005737	cellular_component	cytoplasm
C	0006760	biological_process	folic acid-containing compound metabolic process
C	0016829	molecular_function	lyase activity
C	0016853	molecular_function	isomerase activity
C	0046654	biological_process	tetrahydrofolate biosynthetic process
C	0046656	biological_process	folic acid biosynthetic process
D	0004150	molecular_function	dihydroneopterin aldolase activity
D	0005737	cellular_component	cytoplasm
D	0006760	biological_process	folic acid-containing compound metabolic process
D	0016829	molecular_function	lyase activity
D	0016853	molecular_function	isomerase activity
D	0046654	biological_process	tetrahydrofolate biosynthetic process
D	0046656	biological_process	folic acid biosynthetic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
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

---

site_id	SWS_FT_FI2
Number of Residues	12
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

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 2dhn

Chain	Residue	Details
B	GLU22
B	LYS100

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 2dhn

Chain	Residue	Details
C	GLU22
C	LYS100

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 2dhn

Chain	Residue	Details
D	GLU22
D	LYS100

---

site_id	MCSA1
Number of Residues	2
Details	M-CSA 664

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

---

site_id	MCSA2
Number of Residues	2
Details	M-CSA 664

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

---

site_id	MCSA3
Number of Residues	2
Details	M-CSA 664

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

---

site_id	MCSA4
Number of Residues	2
Details	M-CSA 664

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

---