1ML1

PROTEIN ENGINEERING WITH MONOMERIC TRIOSEPHOSPHATE ISOMERASE: THE MODELLING AND STRUCTURE VERIFICATION OF A SEVEN RESIDUE LOOP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004807	molecular_function	triose-phosphate isomerase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0016853	molecular_function	isomerase activity
A	0019563	biological_process	glycerol catabolic process
A	0020015	cellular_component	glycosome
A	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
C	0004807	molecular_function	triose-phosphate isomerase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006094	biological_process	gluconeogenesis
C	0006096	biological_process	glycolytic process
C	0016853	molecular_function	isomerase activity
C	0019563	biological_process	glycerol catabolic process
C	0020015	cellular_component	glycosome
C	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
E	0004807	molecular_function	triose-phosphate isomerase activity
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006094	biological_process	gluconeogenesis
E	0006096	biological_process	glycolytic process
E	0016853	molecular_function	isomerase activity
E	0019563	biological_process	glycerol catabolic process
E	0020015	cellular_component	glycosome
E	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
G	0004807	molecular_function	triose-phosphate isomerase activity
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0006094	biological_process	gluconeogenesis
G	0006096	biological_process	glycolytic process
G	0016853	molecular_function	isomerase activity
G	0019563	biological_process	glycerol catabolic process
G	0020015	cellular_component	glycosome
G	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
I	0004807	molecular_function	triose-phosphate isomerase activity
I	0005737	cellular_component	cytoplasm
I	0005829	cellular_component	cytosol
I	0006094	biological_process	gluconeogenesis
I	0006096	biological_process	glycolytic process
I	0016853	molecular_function	isomerase activity
I	0019563	biological_process	glycerol catabolic process
I	0020015	cellular_component	glycosome
I	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
K	0004807	molecular_function	triose-phosphate isomerase activity
K	0005737	cellular_component	cytoplasm
K	0005829	cellular_component	cytosol
K	0006094	biological_process	gluconeogenesis
K	0006096	biological_process	glycolytic process
K	0016853	molecular_function	isomerase activity
K	0019563	biological_process	glycerol catabolic process
K	0020015	cellular_component	glycosome
K	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PGA A 600

Chain	Residue
A	ASN11
A	HOH605
A	LYS13
A	HIS95
A	GLU167
A	ILE172
A	GLY173
A	SER213
A	GLY234
A	GLY235

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PGA C 600

Chain	Residue
C	ASN11
C	LYS13
C	HIS95
C	GLU167
C	ILE172
C	GLY173
C	SER213
C	GLY234
C	GLY235
C	HOH604

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PGA E 600

Chain	Residue
E	ASN11
E	LYS13
E	HIS95
E	GLU167
E	ILE172
E	GLY173
E	SER213
E	GLY234
E	GLY235
E	HOH606

---

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PGA G 600

Chain	Residue
G	ASN11
G	LYS13
G	HIS95
G	GLU167
G	ILE172
G	GLY173
G	SER213
G	GLY234
G	GLY235
G	HOH604
G	HOH605
G	HOH608

---

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PGA I 600

Chain	Residue
I	ASN11
I	LYS13
I	HIS95
I	GLU167
I	ILE172
I	GLY173
I	SER213
I	GLY234
I	GLY235
I	HOH607

---

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PGA K 600

Chain	Residue
K	ASN11
K	LYS13
K	HIS95
K	GLU167
K	ILE172
K	GLY173
K	SER213
K	GLY234
K	GLY235
K	HOH607

---

Functional Information from PROSITE/UniProt

site_id	PS00171
Number of Residues	11
Details	TIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG

Chain	Residue	Details
A	ALA165-GLY175

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Electrophile"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1hti

Chain	Residue	Details
A	LYS13
A	HIS95
A	ASN11
A	GLU167
A	GLY173

---

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1hti

Chain	Residue	Details
C	LYS13
C	HIS95
C	ASN11
C	GLU167
C	GLY173

---

site_id	CSA3
Number of Residues	5
Details	Annotated By Reference To The Literature 1hti

Chain	Residue	Details
E	LYS13
E	HIS95
E	ASN11
E	GLU167
E	GLY173

---

site_id	CSA4
Number of Residues	5
Details	Annotated By Reference To The Literature 1hti

Chain	Residue	Details
G	LYS13
G	HIS95
G	ASN11
G	GLU167
G	GLY173

---

site_id	CSA5
Number of Residues	5
Details	Annotated By Reference To The Literature 1hti

Chain	Residue	Details
I	LYS13
I	HIS95
I	ASN11
I	GLU167
I	GLY173

---

site_id	CSA6
Number of Residues	5
Details	Annotated By Reference To The Literature 1hti

Chain	Residue	Details
K	LYS13
K	HIS95
K	ASN11
K	GLU167
K	GLY173

---