Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5MR0

Thermophilic archaeal branched-chain amino acid transaminases from Geoglobus acetivorans and Archaeoglobus fulgidus: biochemical and structural characterisation

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004084	molecular_function	branched-chain-amino-acid:2-oxoglutarate transaminase activity
A	0008652	biological_process	amino acid biosynthetic process
A	0009081	biological_process	branched-chain amino acid metabolic process
A	0009098	biological_process	L-leucine biosynthetic process
A	0009099	biological_process	L-valine biosynthetic 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:2-oxoglutarate transaminase activity
B	0008652	biological_process	amino acid biosynthetic process
B	0009081	biological_process	branched-chain amino acid metabolic process
B	0009098	biological_process	L-leucine biosynthetic process
B	0009099	biological_process	L-valine biosynthetic 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:2-oxoglutarate transaminase activity
C	0008652	biological_process	amino acid biosynthetic process
C	0009081	biological_process	branched-chain amino acid metabolic process
C	0009098	biological_process	L-leucine biosynthetic process
C	0009099	biological_process	L-valine biosynthetic 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:2-oxoglutarate transaminase activity
D	0008652	biological_process	amino acid biosynthetic process
D	0009081	biological_process	branched-chain amino acid metabolic process
D	0009098	biological_process	L-leucine biosynthetic process
D	0009099	biological_process	L-valine biosynthetic 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
E	0003824	molecular_function	catalytic activity
E	0004084	molecular_function	branched-chain-amino-acid:2-oxoglutarate transaminase activity
E	0008652	biological_process	amino acid biosynthetic process
E	0009081	biological_process	branched-chain amino acid metabolic process
E	0009098	biological_process	L-leucine biosynthetic process
E	0009099	biological_process	L-valine biosynthetic process
E	0046394	biological_process	carboxylic acid biosynthetic process
E	0052654	molecular_function	L-leucine:2-oxoglutarate transaminase activity
E	0052655	molecular_function	L-valine:2-oxoglutarate transaminase activity
E	0052656	molecular_function	L-isoleucine:2-oxoglutarate transaminase activity
F	0003824	molecular_function	catalytic activity
F	0004084	molecular_function	branched-chain-amino-acid:2-oxoglutarate transaminase activity
F	0008652	biological_process	amino acid biosynthetic process
F	0009081	biological_process	branched-chain amino acid metabolic process
F	0009098	biological_process	L-leucine biosynthetic process
F	0009099	biological_process	L-valine biosynthetic process
F	0046394	biological_process	carboxylic acid biosynthetic process
F	0052654	molecular_function	L-leucine:2-oxoglutarate transaminase activity
F	0052655	molecular_function	L-valine:2-oxoglutarate transaminase activity
F	0052656	molecular_function	L-isoleucine:2-oxoglutarate transaminase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	binding site for residue PXG A 301

Chain	Residue
A	ARG51
A	LEU206
A	GLY208
A	ILE209
A	THR210
A	GLY245
A	THR246
A	HOH423
A	HOH451
A	HOH466
A	HOH479
A	ARG139
A	HOH505
A	HOH506
B	GLY100
B	LEU101
A	LYS150
A	TYR154
A	ASN157
A	GLU183
A	SER185
A	GLY186
A	ASP187

site_id	AC2
Number of Residues	5
Details	binding site for residue CL A 302

Chain	Residue
A	SER141
A	HOH472
B	SER141
B	HOH452
B	HOH490

site_id	AC3
Number of Residues	3
Details	binding site for residue CL A 303

Chain	Residue
A	ASN229
C	TAM307
C	HOH446

site_id	AC4
Number of Residues	3
Details	binding site for residue PEG A 304

Chain	Residue
A	ASN14
A	LYS116
B	PHE21

site_id	AC5
Number of Residues	5
Details	binding site for residue PEG A 305

Chain	Residue
A	ASN165
A	LYS167
A	GLY168
D	LYS167
D	GLY168

site_id	AC6
Number of Residues	21
Details	binding site for residue PXG B 301

Chain	Residue
A	GLY100
A	LEU101
B	ARG51
B	ARG139
B	LYS150
B	TYR154
B	ASN157
B	GLU183
B	SER185
B	GLY186
B	ASP187
B	LEU206
B	GLY208
B	ILE209
B	THR210
B	GLY245
B	THR246
B	HOH402
B	HOH410
B	HOH427
B	HOH451

site_id	AC7
Number of Residues	3
Details	binding site for residue CL B 302

Chain	Residue
B	ASN229
B	TAM306
E	HOH441

site_id	AC8
Number of Residues	1
Details	binding site for residue PEG B 303

Chain	Residue
B	LYS116

site_id	AC9
Number of Residues	3
Details	binding site for residue PEG B 304

Chain	Residue
A	ALA247
B	ASP98
B	LEU99

site_id	AD1
Number of Residues	2
Details	binding site for residue PEG B 305

Chain	Residue
B	GLY8
B	GLU76

site_id	AD2
Number of Residues	10
Details	binding site for residue TAM B 306

Chain	Residue
B	THR228
B	ASN229
B	CL302
D	THR228
D	ASN229
D	CL302
D	HOH483
E	THR228
E	ASN229
E	CL303

site_id	AD3
Number of Residues	25
Details	binding site for residue PXG C 301

Chain	Residue
C	HOH414
C	HOH467
C	HOH469
D	GLY100
D	LEU101
C	ARG51
C	ARG89
C	ARG139
C	LYS150
C	TYR154
C	ASN157
C	GLU183
C	SER185
C	GLY186
C	ASP187
C	LEU206
C	GLY208
C	ILE209
C	THR210
C	GLY245
C	THR246
C	PEG306
C	HOH406
C	HOH410
C	HOH411

site_id	AD4
Number of Residues	5
Details	binding site for residue CL C 302

Chain	Residue
C	SER141
C	HOH485
D	SER141
D	HOH442
D	HOH496

site_id	AD5
Number of Residues	3
Details	binding site for residue CL C 303

Chain	Residue
C	ASN229
C	TAM307
F	HOH437

site_id	AD6
Number of Residues	1
Details	binding site for residue PEG C 304

Chain	Residue
C	ASN194

site_id	AD7
Number of Residues	3
Details	binding site for residue PEG C 305

Chain	Residue
C	ARG220
E	GLY222
E	HOH503

site_id	AD8
Number of Residues	5
Details	binding site for residue PEG C 306

Chain	Residue
C	TRP118
C	ALA247
C	PXG301
C	HOH506
D	LEU99

site_id	AD9
Number of Residues	12
Details	binding site for residue TAM C 307

Chain	Residue
A	THR228
A	ASN229
A	CL303
A	HOH492
C	THR228
C	ASN229
C	CL303
C	HOH413
C	HOH438
F	THR228
F	ASN229
F	CL301

site_id	AE1
Number of Residues	2
Details	binding site for residue EDO C 308

Chain	Residue
C	ASN14
C	LYS116

site_id	AE2
Number of Residues	22
Details	binding site for residue PXG D 301

Chain	Residue
C	GLY100
C	LEU101
D	ARG51
D	ARG139
D	LYS150
D	TYR154
D	ASN157
D	GLU183
D	SER185
D	GLY186
D	ASP187
D	LEU206
D	GLY208
D	ILE209
D	THR210
D	GLY245
D	THR246
D	HOH402
D	HOH420
D	HOH443
D	HOH460
D	HOH502

site_id	AE3
Number of Residues	3
Details	binding site for residue CL D 302

Chain	Residue
B	TAM306
B	HOH465
D	ASN229

site_id	AE4
Number of Residues	4
Details	binding site for residue PEG D 303

Chain	Residue
D	GLY8
D	PHE10
D	ILE73
D	GLU76

site_id	AE5
Number of Residues	21
Details	binding site for residue PXG E 301

Chain	Residue
E	ARG51
E	ARG139
E	LYS150
E	TYR154
E	ASN157
E	GLU183
E	GLY186
E	ASP187
E	ASN188
E	LEU206
E	GLY208
E	ILE209
E	THR210
E	GLY245
E	THR246
E	HOH426
E	HOH434
E	HOH459
E	HOH461
F	GLY100
F	LEU101

site_id	AE6
Number of Residues	5
Details	binding site for residue CL E 302

Chain	Residue
E	SER141
E	HOH444
E	HOH486
F	SER141
F	HOH481

site_id	AE7
Number of Residues	3
Details	binding site for residue CL E 303

Chain	Residue
B	TAM306
D	HOH427
E	ASN229

site_id	AE8
Number of Residues	3
Details	binding site for residue CL F 301

Chain	Residue
A	HOH442
C	TAM307
F	ASN229

Functional Information from PROSITE/UniProt

site_id	PS00770
Number of Residues	29
Details	AA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EgSgdNIFvvknga......ItTpptinn..LrGItR

Chain	Residue	Details
A	GLU183-ARG211
F	GLU183-ARG211

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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