5LL2

Structure of Isoleucine 2-epimerase from Lactobacillus buchneri (apo form)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008483	molecular_function	transaminase activity
A	0016853	molecular_function	isomerase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042802	molecular_function	identical protein binding
B	0008483	molecular_function	transaminase activity
B	0016853	molecular_function	isomerase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0042802	molecular_function	identical protein binding
C	0008483	molecular_function	transaminase activity
C	0016853	molecular_function	isomerase activity
C	0030170	molecular_function	pyridoxal phosphate binding
C	0042802	molecular_function	identical protein binding
D	0008483	molecular_function	transaminase activity
D	0016853	molecular_function	isomerase activity
D	0030170	molecular_function	pyridoxal phosphate binding
D	0042802	molecular_function	identical protein binding

Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	39
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. FAiDEVnq.GLgRtGkmwaiqqfkdiep...DLMsvGKslaSG

Chain	Residue	Details
A	PHE247-GLY285

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P22256

Chain	Residue	Details
A	GLY115
C	TYR142
C	ASP250
C	THR309
D	GLY115
D	TYR142
D	ASP250
D	THR309
A	TYR142
A	ASP250
A	THR309
B	GLY115
B	TYR142
B	ASP250
B	THR309
C	GLY115

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250|UniProtKB:P22256

Chain	Residue	Details
A	LYS280
B	LYS280
C	LYS280
D	LYS280

---