3AH3

Crystal structure of LR5-1, 3-isopropylmalate dehydrogenase created by directed evolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004449	molecular_function	isocitrate dehydrogenase (NAD+) activity
A	0006099	biological_process	tricarboxylic acid cycle
A	0006102	biological_process	isocitrate metabolic process
A	0008652	biological_process	amino acid biosynthetic process
A	0009085	biological_process	lysine biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0019878	biological_process	lysine biosynthetic process via aminoadipic acid
A	0033708	molecular_function	isocitrate-homoisocitrate dehydrogenase activity
A	0046394	biological_process	carboxylic acid biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0047046	molecular_function	homoisocitrate dehydrogenase activity
B	0004449	molecular_function	isocitrate dehydrogenase (NAD+) activity
B	0006099	biological_process	tricarboxylic acid cycle
B	0006102	biological_process	isocitrate metabolic process
B	0008652	biological_process	amino acid biosynthetic process
B	0009085	biological_process	lysine biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0019878	biological_process	lysine biosynthetic process via aminoadipic acid
B	0033708	molecular_function	isocitrate-homoisocitrate dehydrogenase activity
B	0046394	biological_process	carboxylic acid biosynthetic process
B	0046872	molecular_function	metal ion binding
B	0047046	molecular_function	homoisocitrate dehydrogenase activity
C	0004449	molecular_function	isocitrate dehydrogenase (NAD+) activity
C	0006099	biological_process	tricarboxylic acid cycle
C	0006102	biological_process	isocitrate metabolic process
C	0008652	biological_process	amino acid biosynthetic process
C	0009085	biological_process	lysine biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0019878	biological_process	lysine biosynthetic process via aminoadipic acid
C	0033708	molecular_function	isocitrate-homoisocitrate dehydrogenase activity
C	0046394	biological_process	carboxylic acid biosynthetic process
C	0046872	molecular_function	metal ion binding
C	0047046	molecular_function	homoisocitrate dehydrogenase activity
D	0004449	molecular_function	isocitrate dehydrogenase (NAD+) activity
D	0006099	biological_process	tricarboxylic acid cycle
D	0006102	biological_process	isocitrate metabolic process
D	0008652	biological_process	amino acid biosynthetic process
D	0009085	biological_process	lysine biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0019878	biological_process	lysine biosynthetic process via aminoadipic acid
D	0033708	molecular_function	isocitrate-homoisocitrate dehydrogenase activity
D	0046394	biological_process	carboxylic acid biosynthetic process
D	0046872	molecular_function	metal ion binding
D	0047046	molecular_function	homoisocitrate dehydrogenase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 335

Chain	Residue
A	ARG131
C	LYS144
C	LEU181

---

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO A 336

Chain	Residue
A	GLU298

---

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO A 337

Chain	Residue
A	ILE157

---

site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO A 338

Chain	Residue
A	ILE157

---

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO A 339

Chain	Residue
A	ASN273

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 335

Chain	Residue
D	LYS144
D	LEU181
B	ARG131
B	HOH413

---

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO B 336

Chain	Residue
B	GLU298

---

site_id	AC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO B 337

Chain	Residue
B	ILE157

---

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO B 339

Chain	Residue
B	ALA272
B	ASN273

---

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 335

Chain	Residue
A	LYS144
A	LEU181
C	ARG131
C	HOH351

---

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO C 336

Chain	Residue
C	ASP286
C	GLU298

---

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 335

Chain	Residue
B	LYS144
D	ARG131
D	HOH365

---

site_id	BC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO D 336

Chain	Residue
D	ASP286

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27601325","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4YB4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"27601325","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4YB4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27601325","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4YB4","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Site: {"description":"Important for substrate specificity and discrimination against 3-isopropylmalate"}

Chain

Residue

Details

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