2YFH

Structure of a Chimeric Glutamate Dehydrogenase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004352	molecular_function	L-glutamate dehydrogenase (NAD+) activity
A	0004353	molecular_function	L-glutamate dehydrogenase [NAD(P)+] activity
A	0004354	molecular_function	L-glutamate dehydrogenase (NADP+) activity
A	0005829	cellular_component	cytosol
A	0006520	biological_process	amino acid metabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
A	0055114	biological_process	obsolete oxidation-reduction process
B	0004352	molecular_function	L-glutamate dehydrogenase (NAD+) activity
B	0004353	molecular_function	L-glutamate dehydrogenase [NAD(P)+] activity
B	0004354	molecular_function	L-glutamate dehydrogenase (NADP+) activity
B	0005829	cellular_component	cytosol
B	0006520	biological_process	amino acid metabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
B	0055114	biological_process	obsolete oxidation-reduction process
C	0004352	molecular_function	L-glutamate dehydrogenase (NAD+) activity
C	0004353	molecular_function	L-glutamate dehydrogenase [NAD(P)+] activity
C	0004354	molecular_function	L-glutamate dehydrogenase (NADP+) activity
C	0005829	cellular_component	cytosol
C	0006520	biological_process	amino acid metabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
C	0055114	biological_process	obsolete oxidation-reduction process
D	0004352	molecular_function	L-glutamate dehydrogenase (NAD+) activity
D	0004353	molecular_function	L-glutamate dehydrogenase [NAD(P)+] activity
D	0004354	molecular_function	L-glutamate dehydrogenase (NADP+) activity
D	0005829	cellular_component	cytosol
D	0006520	biological_process	amino acid metabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
D	0055114	biological_process	obsolete oxidation-reduction process
E	0004352	molecular_function	L-glutamate dehydrogenase (NAD+) activity
E	0004353	molecular_function	L-glutamate dehydrogenase [NAD(P)+] activity
E	0004354	molecular_function	L-glutamate dehydrogenase (NADP+) activity
E	0005829	cellular_component	cytosol
E	0006520	biological_process	amino acid metabolic process
E	0016491	molecular_function	oxidoreductase activity
E	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
E	0055114	biological_process	obsolete oxidation-reduction process
F	0004352	molecular_function	L-glutamate dehydrogenase (NAD+) activity
F	0004353	molecular_function	L-glutamate dehydrogenase [NAD(P)+] activity
F	0004354	molecular_function	L-glutamate dehydrogenase (NADP+) activity
F	0005829	cellular_component	cytosol
F	0006520	biological_process	amino acid metabolic process
F	0016491	molecular_function	oxidoreductase activity
F	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
F	0055114	biological_process	obsolete oxidation-reduction process

Functional Information from PROSITE/UniProt

site_id	PS00074
Number of Residues	14
Details	GLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. LpmGGAKgGsdfDP

Chain	Residue	Details
A	LEU120-PRO133

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10011","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8263917","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8263917","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	6
Details	Site: {"description":"Important for catalysis","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 579

Chain	Residue	Details
A	LYS126	electrostatic stabiliser, proton acceptor, proton donor
A	ASP166	proton acceptor, proton donor

---

site_id	MCSA2
Number of Residues	2
Details	M-CSA 579

Chain	Residue	Details
B	LYS126	electrostatic stabiliser, proton acceptor, proton donor
B	ASP166	proton acceptor, proton donor

---

site_id	MCSA3
Number of Residues	2
Details	M-CSA 579

Chain	Residue	Details
C	LYS126	electrostatic stabiliser, proton acceptor, proton donor
C	ASP166	proton acceptor, proton donor

---

site_id	MCSA4
Number of Residues	2
Details	M-CSA 579

Chain	Residue	Details
D	LYS126	electrostatic stabiliser, proton acceptor, proton donor
D	ASP166	proton acceptor, proton donor

---

site_id	MCSA5
Number of Residues	2
Details	M-CSA 579

Chain	Residue	Details
E	LYS126	electrostatic stabiliser, proton acceptor, proton donor
E	ASP166	proton acceptor, proton donor

---

site_id	MCSA6
Number of Residues	2
Details	M-CSA 579

Chain	Residue	Details
F	LYS126	electrostatic stabiliser, proton acceptor, proton donor
F	ASP166	proton acceptor, proton donor

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