7LNM

Ornithine Aminotransferase (OAT) cocrystallized with its inactivator - (1S,3S)-3-amino-4-(difluoromethylene)cyclopentene-1-carboxylic acid

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0004587	molecular_function	L-ornithine transaminase activity
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0007601	biological_process	visual perception
B	0008483	molecular_function	transaminase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0042802	molecular_function	identical protein binding
B	0055129	biological_process	L-proline biosynthetic process
C	0004587	molecular_function	L-ornithine transaminase activity
C	0005515	molecular_function	protein binding
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0007601	biological_process	visual perception
C	0008483	molecular_function	transaminase activity
C	0030170	molecular_function	pyridoxal phosphate binding
C	0042802	molecular_function	identical protein binding
C	0055129	biological_process	L-proline biosynthetic process
E	0004587	molecular_function	L-ornithine transaminase activity
E	0005515	molecular_function	protein binding
E	0005739	cellular_component	mitochondrion
E	0005759	cellular_component	mitochondrial matrix
E	0007601	biological_process	visual perception
E	0008483	molecular_function	transaminase activity
E	0030170	molecular_function	pyridoxal phosphate binding
E	0042802	molecular_function	identical protein binding
E	0055129	biological_process	L-proline biosynthetic process
F	0004587	molecular_function	L-ornithine transaminase activity
F	0005515	molecular_function	protein binding
F	0005739	cellular_component	mitochondrion
F	0005759	cellular_component	mitochondrial matrix
F	0007601	biological_process	visual perception
F	0008483	molecular_function	transaminase activity
F	0030170	molecular_function	pyridoxal phosphate binding
F	0042802	molecular_function	identical protein binding
F	0055129	biological_process	L-proline biosynthetic process
I	0004587	molecular_function	L-ornithine transaminase activity
I	0005515	molecular_function	protein binding
I	0005739	cellular_component	mitochondrion
I	0005759	cellular_component	mitochondrial matrix
I	0007601	biological_process	visual perception
I	0008483	molecular_function	transaminase activity
I	0030170	molecular_function	pyridoxal phosphate binding
I	0042802	molecular_function	identical protein binding
I	0055129	biological_process	L-proline biosynthetic process
J	0004587	molecular_function	L-ornithine transaminase activity
J	0005515	molecular_function	protein binding
J	0005739	cellular_component	mitochondrion
J	0005759	cellular_component	mitochondrial matrix
J	0007601	biological_process	visual perception
J	0008483	molecular_function	transaminase activity
J	0030170	molecular_function	pyridoxal phosphate binding
J	0042802	molecular_function	identical protein binding
J	0055129	biological_process	L-proline biosynthetic process

Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	38
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. FIaDEIqt.GLaRtGrwlavdyenvrp....DIVllGKalsGG

Chain	Residue	Details
B	PHE260-GLY297

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	30
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P29758","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P29758","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	18
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P29758","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"3754226","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 929

Chain

Residue

Details

---

site_id	MCSA2
Number of Residues	3
Details	M-CSA 929

Chain	Residue	Details
B	PHE177	steric role
B	ASP263	electrostatic stabiliser
B	LYS292	covalent catalysis, proton shuttle (general acid/base)

---

site_id	MCSA3
Number of Residues	3
Details	M-CSA 929

Chain	Residue	Details
C	PHE177	steric role
C	ASP263	electrostatic stabiliser
C	LYS292	covalent catalysis, proton shuttle (general acid/base)

---

site_id	MCSA4
Number of Residues	3
Details	M-CSA 929

Chain

Residue

Details

---

site_id	MCSA5
Number of Residues	3
Details	M-CSA 929

Chain	Residue	Details
E	PHE177	steric role
E	ASP263	electrostatic stabiliser
E	LYS292	covalent catalysis, proton shuttle (general acid/base)

---

site_id	MCSA6
Number of Residues	3
Details	M-CSA 929

Chain	Residue	Details
F	PHE177	steric role
F	ASP263	electrostatic stabiliser
F	LYS292	covalent catalysis, proton shuttle (general acid/base)

---