3UHA

Crystal Structure of Saccharopine Dehydrogenase from Saccharomyces cervisiae complexed with NAD.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003729	molecular_function	mRNA binding
A	0004753	molecular_function	saccharopine dehydrogenase activity
A	0004754	molecular_function	saccharopine dehydrogenase (NAD+, L-lysine-forming) activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005777	cellular_component	peroxisome
A	0006553	biological_process	lysine metabolic process
A	0008652	biological_process	amino acid biosynthetic process
A	0009085	biological_process	lysine biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0016558	biological_process	protein import into peroxisome matrix
A	0019878	biological_process	lysine biosynthetic process via aminoadipic acid
B	0003729	molecular_function	mRNA binding
B	0004753	molecular_function	saccharopine dehydrogenase activity
B	0004754	molecular_function	saccharopine dehydrogenase (NAD+, L-lysine-forming) activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005777	cellular_component	peroxisome
B	0006553	biological_process	lysine metabolic process
B	0008652	biological_process	amino acid biosynthetic process
B	0009085	biological_process	lysine biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0016558	biological_process	protein import into peroxisome matrix
B	0019878	biological_process	lysine biosynthetic process via aminoadipic acid

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NAD A 374

Chain	Residue
A	ARG130
A	THR231
A	ILE250
A	TYR251
A	ILE256
A	VAL278
A	ILE318
A	ASP319
A	HIS320
A	LEU321
A	PRO322
A	ALA139
A	ILE199
A	GLY200
A	GLY203
A	ARG204
A	SER205
A	ASP227
A	ILE228

---

site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NAD B 374

Chain	Residue
B	ARG130
B	ALA139
B	ILE199
B	GLY200
B	GLY203
B	ARG204
B	SER205
B	ASP227
B	ILE228
B	THR231
B	CYS249
B	ILE250
B	TYR251
B	ILE256
B	VAL278
B	ILE318
B	ASP319
B	HIS320
B	LEU321
B	PRO322
B	HOH377

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 375

Chain	Residue
A	LYS193
B	LYS193

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:22243403, ECO:0000305|PubMed:17939687

Chain	Residue	Details
A	LYS77
B	LYS77

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:22243403, ECO:0000305|PubMed:17939687

Chain	Residue	Details
A	HIS96
B	HIS96

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:22243403, ECO:0000305|PubMed:17939687, ECO:0007744|PDB:3UH1

Chain	Residue	Details
A	ARG18
A	LYS77
A	ARG131
B	ARG18
B	LYS77
B	ARG131

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0007744|PDB:3UH1

Chain	Residue	Details
A	GLN101
A	PHE135
A	TYR251
A	SER279
B	GLN101
B	PHE135
B	TYR251
B	SER279

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0007744|PDB:3UHA

Chain	Residue	Details
A	ARG130
B	ARG130

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:22243403, ECO:0000305|PubMed:17939687, ECO:0007744|PDB:3UH1, ECO:0007744|PDB:3UHA

Chain	Residue	Details
A	GLY203
A	ASP227
A	THR231
B	GLY203
B	ASP227
B	THR231

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:22243403, ECO:0007744|PDB:3UH1, ECO:0007744|PDB:3UHA

Chain	Residue	Details
A	VAL278
A	ILE318
B	VAL278
B	ILE318

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: N-acetylalanine; partial => ECO:0000269|Ref.4

Chain	Residue	Details
A	ALA2
B	ALA2

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