Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3CSW

Crystal structure of a putative branched-chain amino acid aminotransferase (TM0831) from Thermotoga maritima at 2.15 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004084	molecular_function	branched-chain-amino-acid transaminase activity
A	0008483	molecular_function	transaminase activity
A	0008652	biological_process	amino acid biosynthetic process
A	0009082	biological_process	branched-chain amino acid biosynthetic process
A	0009097	biological_process	isoleucine biosynthetic process
A	0009098	biological_process	L-leucine biosynthetic process
A	0009099	biological_process	L-valine biosynthetic process
A	0016740	molecular_function	transferase activity
A	0019752	biological_process	carboxylic acid metabolic process
A	0046394	biological_process	carboxylic acid biosynthetic process
A	0052654	molecular_function	L-leucine-2-oxoglutarate transaminase activity
A	0052655	molecular_function	L-valine-2-oxoglutarate transaminase activity
A	0052656	molecular_function	L-isoleucine-2-oxoglutarate transaminase activity
B	0003824	molecular_function	catalytic activity
B	0004084	molecular_function	branched-chain-amino-acid transaminase activity
B	0008483	molecular_function	transaminase activity
B	0008652	biological_process	amino acid biosynthetic process
B	0009082	biological_process	branched-chain amino acid biosynthetic process
B	0009097	biological_process	isoleucine biosynthetic process
B	0009098	biological_process	L-leucine biosynthetic process
B	0009099	biological_process	L-valine biosynthetic process
B	0016740	molecular_function	transferase activity
B	0019752	biological_process	carboxylic acid metabolic process
B	0046394	biological_process	carboxylic acid biosynthetic process
B	0052654	molecular_function	L-leucine-2-oxoglutarate transaminase activity
B	0052655	molecular_function	L-valine-2-oxoglutarate transaminase activity
B	0052656	molecular_function	L-isoleucine-2-oxoglutarate transaminase activity
C	0003824	molecular_function	catalytic activity
C	0004084	molecular_function	branched-chain-amino-acid transaminase activity
C	0008483	molecular_function	transaminase activity
C	0008652	biological_process	amino acid biosynthetic process
C	0009082	biological_process	branched-chain amino acid biosynthetic process
C	0009097	biological_process	isoleucine biosynthetic process
C	0009098	biological_process	L-leucine biosynthetic process
C	0009099	biological_process	L-valine biosynthetic process
C	0016740	molecular_function	transferase activity
C	0019752	biological_process	carboxylic acid metabolic process
C	0046394	biological_process	carboxylic acid biosynthetic process
C	0052654	molecular_function	L-leucine-2-oxoglutarate transaminase activity
C	0052655	molecular_function	L-valine-2-oxoglutarate transaminase activity
C	0052656	molecular_function	L-isoleucine-2-oxoglutarate transaminase activity
D	0003824	molecular_function	catalytic activity
D	0004084	molecular_function	branched-chain-amino-acid transaminase activity
D	0008483	molecular_function	transaminase activity
D	0008652	biological_process	amino acid biosynthetic process
D	0009082	biological_process	branched-chain amino acid biosynthetic process
D	0009097	biological_process	isoleucine biosynthetic process
D	0009098	biological_process	L-leucine biosynthetic process
D	0009099	biological_process	L-valine biosynthetic process
D	0016740	molecular_function	transferase activity
D	0019752	biological_process	carboxylic acid metabolic process
D	0046394	biological_process	carboxylic acid biosynthetic process
D	0052654	molecular_function	L-leucine-2-oxoglutarate transaminase activity
D	0052655	molecular_function	L-valine-2-oxoglutarate transaminase activity
D	0052656	molecular_function	L-isoleucine-2-oxoglutarate transaminase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP A 300

Chain	Residue
A	ARG50
A	ASN169
A	LEU188
A	GLY190
A	ILE191
A	THR192
A	THR228
A	LYS133
A	ILE140
A	ARG144
A	GLU164
A	GLY165
A	SER166
A	PHE167
A	SER168

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLP C 300

Chain	Residue
C	ARG50
C	LYS133
C	GLU164
C	SER166
C	PHE167
C	SER168
C	ASN169
C	LEU188
C	GLY190
C	ILE191
C	THR192
C	THR228

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE UNL B 276

Chain	Residue
B	ARG85
B	HIS227
B	THR228
B	SER229

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE UNL C 301

Chain	Residue
C	THR33
C	HIS227
C	THR228
C	SER229

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE UNL A 301

Chain	Residue
A	THR33
A	HIS227
A	THR228
A	SER229

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE UNL D 275

Chain	Residue
D	THR33
D	ARG85
D	HIS227
D	THR228
D	SER229

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CIT A 302

Chain	Residue
A	LEU142
A	ARG145
A	GLU146
B	PHE57
B	PHE58
C	ASP67
C	LYS71

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CIT D 276

Chain	Residue
D	ARG122
D	PRO124
D	ASP125
D	LEU126
D	ASN159

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CIT B 277

Chain	Residue
B	ARG122
B	PRO124
B	ASP125
B	LEU126
B	LEU158
B	ASN159

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MPD A 303

Chain	Residue
A	ASN159
A	ASP184
A	SER185

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MPD A 304

Chain	Residue
A	ASP125
A	PRO129
B	ASN119

site_id	BC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MPD C 303

Chain	Residue
C	ASP184

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD B 278

Chain	Residue
B	LYS52
B	ASP56
B	ASN59
B	LEU60
C	PHE66

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD B 279

Chain	Residue
B	ASP125
B	LEU126
B	SER127
B	THR128
B	PRO129

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MPD D 277

Chain	Residue
C	ASN119
D	PHE57
D	LEU126
D	SER127
D	THR128
D	PRO129

Functional Information from PROSITE/UniProt

site_id	PS00770
Number of Residues	30
Details	AA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EgSfsNVFlvkegk......LiTpsldsgi.LdGItR

Chain	Residue	Details
A	GLU164-ARG193

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1daa

Chain	Residue	Details
A	LYS133
A	GLU164
A	LEU188

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1daa

Chain	Residue	Details
B	LYS133
B	GLU164
B	LEU188

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1daa

Chain	Residue	Details
C	LYS133
C	GLU164
C	LEU188

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1daa

Chain	Residue	Details
D	LYS133
D	GLU164
D	LEU188

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 1daa

Chain	Residue	Details
A	LYS133

site_id	CSA6
Number of Residues	1
Details	Annotated By Reference To The Literature 1daa

Chain	Residue	Details
B	LYS133

site_id	CSA7
Number of Residues	1
Details	Annotated By Reference To The Literature 1daa

Chain	Residue	Details
C	LYS133

site_id	CSA8
Number of Residues	1
Details	Annotated By Reference To The Literature 1daa

Chain	Residue	Details
D	LYS133

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