Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7JX9

The crystal structure of human ornithine aminotransferase with an intermediate bound during inactivation by (1S,3S)-3-amino-4-(hexafluoropropan-2-ylidenyl)-cyclopentane-1-carboxylic acid.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004587	molecular_function	ornithine aminotransferase activity
A	0005515	molecular_function	protein binding
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0007601	biological_process	visual perception
A	0008483	molecular_function	transaminase activity
A	0010121	biological_process	arginine catabolic process to proline via ornithine
A	0019544	biological_process	arginine catabolic process to glutamate
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042802	molecular_function	identical protein binding
A	0055129	biological_process	L-proline biosynthetic process
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	binding site for residue IF1 A 501

Chain	Residue
A	TYR55
A	ILE265
A	GLN266
A	LYS292
A	SER321
A	THR322
A	ARG413
A	HOH611
A	HOH614
A	HOH665
A	HOH672
A	TYR85
A	HOH722
A	HOH725
A	HOH729
A	HOH738
A	GLY142
A	VAL143
A	PHE177
A	TRP178
A	GLU230
A	GLU235
A	ASP263

site_id	AC2
Number of Residues	14
Details	binding site for residue VLS A 502

Chain	Residue
A	SER186
A	PHE200
A	MET201
A	PRO202
A	GLY203
A	PHE204
A	HOH627
A	HOH644
A	HOH655
A	HOH671
A	HOH691
A	HOH717
C	ARG217
C	ALA218

site_id	AC3
Number of Residues	22
Details	binding site for residue IF1 B 501

Chain	Residue
B	TYR55
B	TYR85
B	GLY142
B	VAL143
B	PHE177
B	TRP178
B	GLU230
B	GLU235
B	ASP263
B	ILE265
B	GLN266
B	LYS292
B	ARG413
B	HOH604
B	HOH648
B	HOH661
B	HOH683
B	HOH685
B	HOH731
C	SER321
C	THR322
C	HOH628

site_id	AC4
Number of Residues	23
Details	binding site for residue IF1 C 501

Chain	Residue
B	SER321
B	THR322
B	HOH625
C	TYR55
C	TYR85
C	GLY142
C	VAL143
C	PHE177
C	TRP178
C	GLU235
C	ASP263
C	ILE265
C	GLN266
C	LYS292
C	ARG413
C	HOH638
C	HOH643
C	HOH671
C	HOH706
C	HOH709
C	HOH728
C	HOH745
C	HOH746

site_id	AC5
Number of Residues	13
Details	binding site for residue VLS C 502

Chain	Residue
A	ARG217
A	ALA218
A	HOH682
C	SER186
C	PHE200
C	MET201
C	PRO202
C	GLY203
C	PHE204
C	HOH636
C	HOH650
C	HOH653
C	HOH688

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
A	PHE260-GLY297

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	15
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P29758

Chain	Residue	Details
A	LYS49
B	LYS421
C	LYS49
C	LYS66
C	LYS386
C	LYS392
C	LYS421
A	LYS66
A	LYS386
A	LYS392
A	LYS421
B	LYS49
B	LYS66
B	LYS386
B	LYS392

site_id	SWS_FT_FI2
Number of Residues	3
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:P29758

Chain	Residue	Details
A	LYS102
B	LYS102
C	LYS102

site_id	SWS_FT_FI3
Number of Residues	9
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P29758

Chain	Residue	Details
A	LYS107
A	LYS362
A	LYS405
B	LYS107
B	LYS362
B	LYS405
C	LYS107
C	LYS362
C	LYS405

site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269\|PubMed:3754226

Chain	Residue	Details
A	LYS292
B	LYS292
C	LYS292

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 929

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

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)

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