Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2OAT

ORNITHINE AMINOTRANSFERASE COMPLEXED WITH 5-FLUOROMETHYLORNITHINE

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	0016740	molecular_function	transferase activity
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	0016740	molecular_function	transferase activity
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	0016740	molecular_function	transferase activity
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	21
Details	BINDING SITE FOR RESIDUE PFM A 440

Chain	Residue
A	ARG180
A	GLU230
A	GLU235
A	ASP263
A	GLN266
A	LYS292
A	HOH473
A	HOH514
A	HOH543
A	HOH545
A	HOH643
B	GLY320
B	SER321
B	THR322
B	HOH524
A	TYR55
A	THR141
A	GLY142
A	VAL143
A	PHE177
A	TRP178

site_id	AC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE PFM B 440

Chain	Residue
A	GLY320
A	SER321
A	THR322
A	HOH512
A	HOH644
B	TYR55
B	TYR85
B	THR141
B	GLY142
B	VAL143
B	PHE177
B	TRP178
B	ARG180
B	GLU230
B	ASP263
B	ILE265
B	GLN266
B	LYS292
B	HOH444
B	HOH489
B	HOH526
B	HOH555
B	HOH558

site_id	AC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE PFM C 440

Chain	Residue
C	TYR55
C	TYR85
C	THR141
C	GLY142
C	VAL143
C	PHE177
C	TRP178
C	ARG180
C	GLU230
C	ASP263
C	ILE265
C	GLN266
C	LYS292
C	GLY320
C	SER321
C	THR322
C	HOH478
C	HOH507
C	HOH522
C	HOH524
C	HOH556
C	HOH559
C	HOH673

site_id	FMA
Number of Residues	1
Details	THE INHIBITOR-COFACTOR ADDUCT HAS AN ABSORPTION MAXIMUM AT 458NM AND IS NON-COVALENTLY BOUND TO THE ACTIVE SITE RESIDUES.

Chain	Residue
A	PFM440

site_id	FMB
Number of Residues	1
Details	THE INHIBITOR-COFACTOR ADDUCT HAS AN ABSORPTION MAXIMUM AT 458NM AND IS NON-COVALENTLY BOUND TO THE ACTIVE SITE RESIDUES.

Chain	Residue
B	PFM440

site_id	FMC
Number of Residues	1
Details	THE INHIBITOR-COFACTOR ADDUCT HAS AN ABSORPTION MAXIMUM AT 458NM AND IS NON-COVALENTLY BOUND TO THE ACTIVE SITE RESIDUES.

Chain	Residue
C	PFM440

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)