Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

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	ornithine aminotransferase activity
B	0005515	molecular_function	protein binding
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0007601	biological_process	visual perception
B	0008483	molecular_function	transaminase activity
B	0010121	biological_process	arginine catabolic process to proline via ornithine
B	0019544	biological_process	arginine catabolic process to glutamate
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	ornithine aminotransferase activity
C	0005515	molecular_function	protein binding
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0007601	biological_process	visual perception
C	0008483	molecular_function	transaminase activity
C	0010121	biological_process	arginine catabolic process to proline via ornithine
C	0019544	biological_process	arginine catabolic process to glutamate
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	ornithine aminotransferase activity
E	0005515	molecular_function	protein binding
E	0005654	cellular_component	nucleoplasm
E	0005737	cellular_component	cytoplasm
E	0005739	cellular_component	mitochondrion
E	0005759	cellular_component	mitochondrial matrix
E	0007601	biological_process	visual perception
E	0008483	molecular_function	transaminase activity
E	0010121	biological_process	arginine catabolic process to proline via ornithine
E	0019544	biological_process	arginine catabolic process to glutamate
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	ornithine aminotransferase activity
F	0005515	molecular_function	protein binding
F	0005654	cellular_component	nucleoplasm
F	0005737	cellular_component	cytoplasm
F	0005739	cellular_component	mitochondrion
F	0005759	cellular_component	mitochondrial matrix
F	0007601	biological_process	visual perception
F	0008483	molecular_function	transaminase activity
F	0010121	biological_process	arginine catabolic process to proline via ornithine
F	0019544	biological_process	arginine catabolic process to glutamate
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	ornithine aminotransferase activity
I	0005515	molecular_function	protein binding
I	0005654	cellular_component	nucleoplasm
I	0005737	cellular_component	cytoplasm
I	0005739	cellular_component	mitochondrion
I	0005759	cellular_component	mitochondrial matrix
I	0007601	biological_process	visual perception
I	0008483	molecular_function	transaminase activity
I	0010121	biological_process	arginine catabolic process to proline via ornithine
I	0019544	biological_process	arginine catabolic process to glutamate
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	ornithine aminotransferase activity
J	0005515	molecular_function	protein binding
J	0005654	cellular_component	nucleoplasm
J	0005737	cellular_component	cytoplasm
J	0005739	cellular_component	mitochondrion
J	0005759	cellular_component	mitochondrial matrix
J	0007601	biological_process	visual perception
J	0008483	molecular_function	transaminase activity
J	0010121	biological_process	arginine catabolic process to proline via ornithine
J	0019544	biological_process	arginine catabolic process to glutamate
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

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	30
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P29758

Chain	Residue	Details
C	LYS49
C	LYS66
C	LYS386
C	LYS392
C	LYS421
E	LYS49
E	LYS66
E	LYS386
E	LYS392
E	LYS421
F	LYS49
F	LYS66
F	LYS386
F	LYS392
F	LYS421
I	LYS49
I	LYS66
I	LYS386
I	LYS392
I	LYS421
J	LYS49
J	LYS66
J	LYS386
J	LYS392
J	LYS421
B	LYS49
B	LYS66
B	LYS386
B	LYS392
B	LYS421

site_id	SWS_FT_FI2
Number of Residues	6
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:P29758

Chain	Residue	Details
C	LYS102
E	LYS102
F	LYS102
I	LYS102
J	LYS102
B	LYS102

site_id	SWS_FT_FI3
Number of Residues	18
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P29758

Chain	Residue	Details
C	LYS107
C	LYS362
C	LYS405
E	LYS107
E	LYS362
E	LYS405
F	LYS107
F	LYS362
F	LYS405
I	LYS107
I	LYS362
I	LYS405
J	LYS107
J	LYS362
J	LYS405
B	LYS107
B	LYS362
B	LYS405

site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269\|PubMed:3754226

Chain	Residue	Details
C	LYS292
E	LYS292
F	LYS292
I	LYS292
J	LYS292
B	LYS292

Catalytic Information from CSA

site_id	MCSA1
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	MCSA2
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	MCSA3
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	MCSA4
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)

site_id	MCSA5
Number of Residues	3
Details	M-CSA 929

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

site_id	MCSA6
Number of Residues	3
Details	M-CSA 929

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)