Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1I1M

CRYSTAL STRUCTURE OF ESCHERICHIA 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	0016740	molecular_function	transferase activity
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
A	1901566	biological_process	organonitrogen compound biosynthetic process
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	0016740	molecular_function	transferase activity
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
B	1901566	biological_process	organonitrogen compound biosynthetic process
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	0016740	molecular_function	transferase activity
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
C	1901566	biological_process	organonitrogen compound biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP A 413

Chain	Residue
A	ARG59
A	THR221
A	GLY256
A	THR257
A	4MV414
A	HOH417
A	HOH422
A	LYS159
A	TYR164
A	GLU193
A	GLY196
A	GLU197
A	LEU217
A	GLY219
A	ILE220

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 4MV A 414

Chain	Residue
A	GLY38
A	TYR95
A	LYS159
A	TYR164
A	GLY196
A	THR257
A	ALA258
A	PLP413
A	HOH434

site_id	AC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP B 913

Chain	Residue
B	HOH36
B	HOH46
B	HOH101
B	ARG559
B	LYS659
B	TYR664
B	GLU693
B	GLY696
B	GLU697
B	LEU717
B	GLY719
B	ILE720
B	THR721
B	GLY756
B	THR757
B	4MV914

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE 4MV B 914

Chain	Residue
B	HOH127
B	TYR595
B	TYR664
B	THR757
B	ALA758
B	PLP913

site_id	AC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP C 1413

Chain	Residue
C	HOH2
C	HOH25
C	ARG1059
C	LYS1159
C	TYR1164
C	GLU1193
C	GLY1196
C	GLU1197
C	LEU1217
C	GLY1219
C	ILE1220
C	THR1221
C	GLY1256
C	THR1257
C	4MV1414

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 4MV C 1414

Chain	Residue
C	HOH117
C	TYR1095
C	LYS1159
C	GLY1196
C	THR1257
C	ALA1258
C	PLP1413

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	LYS159
B	LYS659
C	LYS1159

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	1
Details	M-CSA 813

Chain	Residue	Details
A	LYS159	proton shuttle (general acid/base)

site_id	MCSA2
Number of Residues	1
Details	M-CSA 813

Chain	Residue	Details
B	LYS659	proton shuttle (general acid/base)

site_id	MCSA3
Number of Residues	1
Details	M-CSA 813

Chain	Residue	Details
C	LYS1159	proton shuttle (general acid/base)

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