Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1IYE

CRYSTAL STRUCTURE OF ESCHELICHIA COLI BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE

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	0042802	molecular_function	identical protein binding
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	0042802	molecular_function	identical protein binding
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	0042802	molecular_function	identical protein binding
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	26
Details	BINDING SITE FOR RESIDUE PGU A 513

Chain	Residue
A	GLY38
A	ALA195
A	GLY196
A	GLU197
A	ASN198
A	LEU217
A	GLY219
A	ILE220
A	THR221
A	GLY256
A	THR257
A	ARG59
A	ALA258
A	HOH539
A	HOH546
A	HOH559
B	TYR31
B	GLY108
B	VAL109
A	TYR95
A	ARG97
A	TYR129
A	ARG148
A	LYS159
A	TYR164
A	GLU193

site_id	AC2
Number of Residues	26
Details	BINDING SITE FOR RESIDUE PGU B 913

Chain	Residue
A	TYR31
A	GLY108
A	VAL109
B	GLY38
B	ARG59
B	TYR95
B	ARG97
B	TYR129
B	ARG148
B	LYS159
B	TYR164
B	GLU193
B	ALA195
B	GLY196
B	GLU197
B	ASN198
B	LEU217
B	GLY219
B	ILE220
B	THR221
B	GLY256
B	THR257
B	ALA258
B	HOH922
B	HOH927
B	HOH932

site_id	AC3
Number of Residues	26
Details	BINDING SITE FOR RESIDUE PGU C 1413

Chain	Residue
C	TYR31
C	GLY38
C	ARG59
C	TYR95
C	ARG97
C	GLY108
C	VAL109
C	TYR129
C	ARG148
C	LYS159
C	TYR164
C	GLU193
C	ALA195
C	GLY196
C	GLU197
C	ASN198
C	LEU217
C	GLY219
C	ILE220
C	THR221
C	GLY256
C	THR257
C	ALA258
C	HOH1425
C	HOH1430
C	HOH1448

Functional Information from PROSITE/UniProt

site_id	PS00770
Number of Residues	30
Details	AA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EgAgeNLFevkdgv......LfTppftssa.LpGItR

Chain	Residue	Details
A	GLU193-ARG222

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	MOD_RES: N6-(pyridoxal phosphate)lysine

Chain	Residue	Details
A	ALA160
B	ALA160
C	ALA160

Catalytic Information from CSA

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

Chain	Residue	Details
A	LYS159

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

Chain	Residue	Details
B	LYS159

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

Chain	Residue	Details
C	LYS159

site_id	MCSA1
Number of Residues	1
Details	M-CSA 813

Chain	Residue	Details
A	ALA160	proton shuttle (general acid/base)

site_id	MCSA2
Number of Residues	1
Details	M-CSA 813

Chain	Residue	Details
B	ALA160	proton shuttle (general acid/base)

site_id	MCSA3
Number of Residues	1
Details	M-CSA 813

Chain	Residue	Details
C	ALA160	proton shuttle (general acid/base)

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