Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6THQ

Crystal structure of branched-chain aminotransferase from thermophilic archaea Thermoproteus uzoniensis with norvaline

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	0005829	cellular_component	cytosol
A	0006532	biological_process	aspartate biosynthetic process
A	0008483	molecular_function	transaminase activity
A	0008652	biological_process	amino acid biosynthetic process
A	0009081	biological_process	branched-chain amino acid metabolic 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	valine biosynthetic process
A	0046394	biological_process	carboxylic acid biosynthetic process
A	0050048	molecular_function	L-leucine:2-oxoglutarate aminotransferase activity
A	0052654	molecular_function	L-leucine transaminase activity
A	0052655	molecular_function	L-valine transaminase activity
A	0052656	molecular_function	L-isoleucine transaminase activity
B	0003824	molecular_function	catalytic activity
B	0004084	molecular_function	branched-chain-amino-acid transaminase activity
B	0005829	cellular_component	cytosol
B	0006532	biological_process	aspartate biosynthetic process
B	0008483	molecular_function	transaminase activity
B	0008652	biological_process	amino acid biosynthetic process
B	0009081	biological_process	branched-chain amino acid metabolic 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	valine biosynthetic process
B	0046394	biological_process	carboxylic acid biosynthetic process
B	0050048	molecular_function	L-leucine:2-oxoglutarate aminotransferase activity
B	0052654	molecular_function	L-leucine transaminase activity
B	0052655	molecular_function	L-valine transaminase activity
B	0052656	molecular_function	L-isoleucine transaminase activity
C	0003824	molecular_function	catalytic activity
C	0004084	molecular_function	branched-chain-amino-acid transaminase activity
C	0005829	cellular_component	cytosol
C	0006532	biological_process	aspartate biosynthetic process
C	0008483	molecular_function	transaminase activity
C	0008652	biological_process	amino acid biosynthetic process
C	0009081	biological_process	branched-chain amino acid metabolic 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	valine biosynthetic process
C	0046394	biological_process	carboxylic acid biosynthetic process
C	0050048	molecular_function	L-leucine:2-oxoglutarate aminotransferase activity
C	0052654	molecular_function	L-leucine transaminase activity
C	0052655	molecular_function	L-valine transaminase activity
C	0052656	molecular_function	L-isoleucine transaminase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue PLP A 301

Chain	Residue
A	HIS51
A	ILE211
A	THR212
A	THR248
A	PY5302
A	HOH401
A	HOH430
A	ARG54
A	ARG139
A	LYS150
A	TYR155
A	GLU184
A	SER186
A	LEU208
A	GLY210

site_id	AC2
Number of Residues	21
Details	binding site for residue PY5 A 302

Chain	Residue
A	GLY33
A	ARG54
A	TYR91
A	ARG139
A	LYS150
A	TYR155
A	GLU184
A	SER186
A	GLY187
A	GLU188
A	ASN189
A	GLY210
A	ILE211
A	THR212
A	GLY247
A	THR248
A	ALA249
A	PLP301
A	HOH401
A	HOH430
A	HOH442

site_id	AC3
Number of Residues	16
Details	binding site for residue PLP B 301

Chain	Residue
B	HIS51
B	ARG54
B	ARG139
B	LYS150
B	TYR155
B	GLU184
B	ASN189
B	LEU208
B	GLY210
B	ILE211
B	THR212
B	GLY247
B	THR248
B	PY5302
B	HOH407
B	HOH429

site_id	AC4
Number of Residues	19
Details	binding site for residue PY5 B 302

Chain	Residue
B	GLY33
B	ARG54
B	TYR91
B	LYS150
B	TYR155
B	GLU184
B	SER186
B	GLY187
B	GLU188
B	GLY210
B	ILE211
B	THR212
B	GLY247
B	THR248
B	ALA249
B	PLP301
B	HOH402
B	HOH407
B	HOH429

site_id	AC5
Number of Residues	20
Details	binding site for residue PY5 C 302

Chain	Residue
B	ILE103
C	ARG54
C	TYR91
C	ARG139
C	LYS150
C	TYR155
C	GLU184
C	SER186
C	GLY187
C	GLU188
C	ASN189
C	GLY210
C	ILE211
C	THR212
C	GLY247
C	THR248
C	ALA249
C	PLP301
C	HOH408
C	HOH413

site_id	AC6
Number of Residues	20
Details	binding site for Di-peptide PLP C 301 and LYS C 150

Chain	Residue
C	TYR155
C	GLU184
C	GLU188
C	ASN189
C	LEU208
C	GLY210
C	ILE211
C	THR212
C	THR248
C	PY5302
C	HOH408
C	HOH413
C	VAL30
C	PHE31
C	HIS51
C	ARG54
C	SER58
C	ARG139
C	ALA149
C	ALA151

Functional Information from PROSITE/UniProt

site_id	PS00445
Number of Residues	21
Details	FGGY_KINASES_2 FGGY family of carbohydrate kinases signature 2. AkIIGLdvpytae.ELSKAVVE

Chain	Residue	Details
A	ALA59-GLU79

site_id	PS00770
Number of Residues	30
Details	AA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EgSgeNIFivrrgv......LmTppledgi.LeGItR

Chain	Residue	Details
A	GLU184-ARG213

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)