2V2H

The A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase (TIM) induces a more closed conformation of this hinge region in dimeric and monomeric TIM

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
B	0004807	molecular_function	triose-phosphate isomerase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006094	biological_process	gluconeogenesis
B	0006096	biological_process	glycolytic process
B	0016853	molecular_function	isomerase activity
B	0019563	biological_process	glycerol catabolic process
B	0020015	cellular_component	glycosome
B	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

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PGA A1251

Chain	Residue
A	ASN11
A	GLY234
A	GLY235
A	HOH2253
A	HOH2287
A	HOH2288
A	HOH2289
A	LYS13
A	HIS95
A	GLU167
A	ALA171
A	ILE172
A	GLY173
A	GLY212
A	SER213

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PGA B1251

Chain	Residue
B	ASN11
B	LYS13
B	HIS95
B	GLU167
B	ALA171
B	ILE172
B	GLY173
B	GLY212
B	SER213
B	GLY234
B	GLY235
B	HOH2246
B	HOH2284
B	HOH2285
B	HOH2286

---

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PGA C1251

Chain	Residue
C	ASN11
C	LYS13
C	HIS95
C	GLU167
C	ALA171
C	ILE172
C	GLY173
C	GLY212
C	SER213
C	GLY234
C	GLY235
C	HOH2270
C	HOH2271
C	HOH2272
C	HOH2273

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL C1252

Chain	Residue
B	LYS52
B	PHE86
C	LEU131
C	TRP170

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL B1252

Chain	Residue
A	LYS52
A	PHE86
B	LEU131
B	TRP170

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A1252

Chain	Residue
A	LEU131
C	LYS52
C	PHE86

---

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	3
Details	ACT_SITE: Electrophile

Chain	Residue	Details
A	HIS95
B	HIS95
C	HIS95

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	GLU167
B	GLU167
C	GLU167

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING:

Chain	Residue	Details
A	ASN11
A	LYS13
B	ASN11
B	LYS13
C	ASN11
C	LYS13

---

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
B	LYS13
B	HIS95
B	ASN11
B	GLU167
B	GLY173

---

site_id	CSA3
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

---