Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6RL5

The first crystal structure of the DABA aminotransferase EctB in the ectoine biosynthesis pathway of the model organism Chromohalobacter salexigens DSM 3034

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008483	molecular_function	transaminase activity
A	0009058	biological_process	biosynthetic process
A	0019491	biological_process	ectoine biosynthetic process
A	0030170	molecular_function	pyridoxal phosphate binding
A	0045303	molecular_function	diaminobutyrate-2-oxoglutarate transaminase activity
A	0047307	molecular_function	diaminobutyrate-pyruvate transaminase activity
B	0008483	molecular_function	transaminase activity
B	0009058	biological_process	biosynthetic process
B	0019491	biological_process	ectoine biosynthetic process
B	0030170	molecular_function	pyridoxal phosphate binding
B	0045303	molecular_function	diaminobutyrate-2-oxoglutarate transaminase activity
B	0047307	molecular_function	diaminobutyrate-pyruvate transaminase activity
C	0008483	molecular_function	transaminase activity
C	0009058	biological_process	biosynthetic process
C	0019491	biological_process	ectoine biosynthetic process
C	0030170	molecular_function	pyridoxal phosphate binding
C	0045303	molecular_function	diaminobutyrate-2-oxoglutarate transaminase activity
C	0047307	molecular_function	diaminobutyrate-pyruvate transaminase activity
D	0008483	molecular_function	transaminase activity
D	0009058	biological_process	biosynthetic process
D	0019491	biological_process	ectoine biosynthetic process
D	0030170	molecular_function	pyridoxal phosphate binding
D	0045303	molecular_function	diaminobutyrate-2-oxoglutarate transaminase activity
D	0047307	molecular_function	diaminobutyrate-pyruvate transaminase activity
E	0008483	molecular_function	transaminase activity
E	0009058	biological_process	biosynthetic process
E	0019491	biological_process	ectoine biosynthetic process
E	0030170	molecular_function	pyridoxal phosphate binding
E	0045303	molecular_function	diaminobutyrate-2-oxoglutarate transaminase activity
E	0047307	molecular_function	diaminobutyrate-pyruvate transaminase activity
F	0008483	molecular_function	transaminase activity
F	0009058	biological_process	biosynthetic process
F	0019491	biological_process	ectoine biosynthetic process
F	0030170	molecular_function	pyridoxal phosphate binding
F	0045303	molecular_function	diaminobutyrate-2-oxoglutarate transaminase activity
F	0047307	molecular_function	diaminobutyrate-pyruvate transaminase activity
G	0008483	molecular_function	transaminase activity
G	0009058	biological_process	biosynthetic process
G	0019491	biological_process	ectoine biosynthetic process
G	0030170	molecular_function	pyridoxal phosphate binding
G	0045303	molecular_function	diaminobutyrate-2-oxoglutarate transaminase activity
G	0047307	molecular_function	diaminobutyrate-pyruvate transaminase activity
H	0008483	molecular_function	transaminase activity
H	0009058	biological_process	biosynthetic process
H	0019491	biological_process	ectoine biosynthetic process
H	0030170	molecular_function	pyridoxal phosphate binding
H	0045303	molecular_function	diaminobutyrate-2-oxoglutarate transaminase activity
H	0047307	molecular_function	diaminobutyrate-pyruvate transaminase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue PLP A 501

Chain	Residue
A	GLY111
B	THR296
A	THR112
A	PHE138
A	HIS139
A	ASP238
A	ILE240
A	GLN241
A	LYS267
B	GLY295

site_id	AC2
Number of Residues	12
Details	binding site for residue PLP E 501

Chain	Residue
E	GLY111
E	THR112
E	PHE138
E	HIS139
E	ASP238
E	ILE240
E	GLN241
E	LYS267
E	HOH602
E	HOH624
F	GLY295
F	THR296

site_id	AC3
Number of Residues	12
Details	binding site for residue PLP H 501

Chain	Residue
G	GLY295
G	THR296
H	THR110
H	GLY111
H	THR112
H	PHE138
H	HIS139
H	GLU205
H	ASP238
H	ILE240
H	GLN241
H	LYS267

site_id	AC4
Number of Residues	18
Details	binding site for Di-peptide PLP B 501 and LYS B 267

Chain	Residue
A	GLY295
A	THR296
B	ALA47
B	THR49
B	GLY111
B	THR112
B	PHE138
B	GLU205
B	ASP238
B	ILE240
B	GLN241
B	SER266
B	SER268
B	LEU269
B	HOH601
B	HOH602
B	HOH616
B	HOH634

site_id	AC5
Number of Residues	17
Details	binding site for Di-peptide PLP C 501 and LYS C 267

Chain	Residue
C	ALA47
C	GLY48
C	THR49
C	THR110
C	GLY111
C	THR112
C	PHE138
C	HIS139
C	ASP238
C	ILE240
C	GLN241
C	SER266
C	SER268
C	LEU269
D	GLY295
D	THR296
D	PHE297

site_id	AC6
Number of Residues	17
Details	binding site for Di-peptide PLP D 501 and LYS D 267

Chain	Residue
C	THR296
C	PHE297
D	ALA47
D	GLY48
D	THR49
D	GLY111
D	THR112
D	PHE138
D	GLU205
D	ASP238
D	ILE240
D	GLN241
D	SER266
D	SER268
D	LEU269
D	HOH604
D	HOH605

site_id	AC7
Number of Residues	16
Details	binding site for Di-peptide PLP F 501 and LYS F 267

Chain	Residue
F	SER266
F	SER268
F	LEU269
E	GLY295
E	THR296
E	PHE297
F	ALA47
F	GLY48
F	THR49
F	THR110
F	GLY111
F	THR112
F	PHE138
F	ASP238
F	ILE240
F	GLN241

site_id	AC8
Number of Residues	17
Details	binding site for Di-peptide PLP G 501 and LYS G 267

Chain	Residue
G	ALA47
G	THR49
G	GLY111
G	THR112
G	PHE138
G	HIS139
G	ASP238
G	ILE240
G	GLN241
G	SER266
G	SER268
G	LEU269
G	HOH613
G	HOH616
G	HOH625
H	THR296
H	PHE297

Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	37
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIvDDIqa.GCgRtGkffsfehagitp....DIVtnSKsl.SG

Chain	Residue	Details
A	LEU235-GLY271

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255

Chain	Residue	Details
A	LYS267
B	LYS267
C	LYS267
D	LYS267
E	LYS267
F	LYS267
G	LYS267
H	LYS267

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