1IYD

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	13
Details	BINDING SITE FOR RESIDUE PLP A 413

Chain	Residue
A	ARG59
A	THR221
A	THR257
A	HOH447
A	HOH480
A	LYS159
A	TYR164
A	GLU193
A	GLY196
A	GLU197
A	LEU217
A	GLY219
A	ILE220

---

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP B 913

Chain	Residue
B	ARG59
B	ARG148
B	LYS159
B	TYR164
B	GLU193
B	GLY196
B	GLU197
B	LEU217
B	GLY219
B	ILE220
B	THR221
B	GLY256
B	THR257
B	HOH921
B	HOH931
B	HOH955

---

site_id	AC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP C 1413

Chain	Residue
C	ARG59
C	ARG148
C	LYS159
C	TYR164
C	GLU193
C	GLU197
C	LEU217
C	GLY219
C	ILE220
C	THR221
C	GLY256
C	THR257
C	GUA1414
C	HOH1415
C	HOH1424
C	HOH1439

---

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GUA A 414

Chain	Residue
A	GLY38
A	TYR95
A	ARG97
A	TYR129
A	TYR164
A	THR257
A	ALA258
A	HOH454
B	TYR31
B	MET107
B	VAL109

---

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GUA B 914

Chain	Residue
A	TYR31
A	MET107
A	VAL109
B	GLY38
B	TYR95
B	ARG97
B	TYR129
B	THR257
B	ALA258
B	HOH924

---

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GUA C 1414

Chain	Residue
C	TYR31
C	GLY38
C	TYR95
C	ARG97
C	MET107
C	VAL109
C	TYR129
C	THR257
C	ALA258
C	PLP1413
C	HOH1491

---

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

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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

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 12667063

Chain	Residue	Details
A	LYS159

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site_id	CSA2
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 12667063

Chain	Residue	Details
B	LYS159

---

site_id	CSA3
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 12667063

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)

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site_id	MCSA2
Number of Residues	1
Details	M-CSA 813

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

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site_id	MCSA3
Number of Residues	1
Details	M-CSA 813

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

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