2VFG

Crystal structure of the F96H mutant of Plasmodium falciparum triosephosphate isomerase with 3-phosphoglycerate bound at the dimer interface

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004807	molecular_function	triose-phosphate isomerase activity
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0016853	molecular_function	isomerase activity
A	0042802	molecular_function	identical protein binding
B	0004807	molecular_function	triose-phosphate isomerase activity
B	0006094	biological_process	gluconeogenesis
B	0006096	biological_process	glycolytic process
B	0016853	molecular_function	isomerase activity
B	0042802	molecular_function	identical protein binding
C	0004807	molecular_function	triose-phosphate isomerase activity
C	0006094	biological_process	gluconeogenesis
C	0006096	biological_process	glycolytic process
C	0016853	molecular_function	isomerase activity
C	0042802	molecular_function	identical protein binding
D	0004807	molecular_function	triose-phosphate isomerase activity
D	0006094	biological_process	gluconeogenesis
D	0006096	biological_process	glycolytic process
D	0016853	molecular_function	isomerase activity
D	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE 3PG A 1249

Chain	Residue
A	ASN65
A	HOH2170
A	HOH2171
A	HOH2172
A	HOH2173
B	TYR101
B	PHE102
B	HIS103
A	LYS68
A	ARG98
A	PHE102
A	HIS103
A	GLU104
A	ASP108
A	LYS112
A	HOH2075

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 3PG B 1249

Chain	Residue
A	TYR101
A	PHE102
A	HIS103
A	HOH2172
A	HOH2173
B	ASN65
B	LYS68
B	ARG98
B	PHE102
B	HIS103
B	GLU104
B	ASP108
B	LYS112
B	HOH2060
B	HOH2087

---

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 3PG C 1249

Chain	Residue
C	ASN65
C	LYS68
C	ARG98
C	PHE102
C	HIS103
C	GLU104
C	ASP108
C	LYS112
C	HOH2069
C	HOH2153
D	TYR101
D	PHE102
D	HIS103
D	HOH2191
D	HOH2192

---

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE 3PG D 1249

Chain	Residue
C	TYR101
C	PHE102
C	HIS103
D	ASN65
D	LYS68
D	ARG98
D	PHE102
D	HIS103
D	GLU104
D	ASP108
D	LYS112
D	HOH2071
D	HOH2190
D	HOH2191
D	HOH2192
D	HOH2193

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL163-GLY173

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Electrophile => ECO:0000255|PROSITE-ProRule:PRU10127

Chain	Residue	Details
A	HIS95
B	HIS95
C	HIS95
D	HIS95

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10127

Chain	Residue	Details
A	GLU165
B	GLU165
C	GLU165
D	GLU165

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:12454456, ECO:0000269|PubMed:14563846, ECO:0000269|PubMed:19622869, ECO:0007744|PDB:1M7O, ECO:0007744|PDB:1O5X, ECO:0007744|PDB:2VFI

Chain	Residue	Details
A	ASN10
B	ASN10
C	ASN10
D	ASN10

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:12403619, ECO:0000269|PubMed:15465054, ECO:0000269|PubMed:19622869, ECO:0007744|PDB:1LYX, ECO:0007744|PDB:1LZO, ECO:0007744|PDB:1WOA, ECO:0007744|PDB:2VFI

Chain	Residue	Details
A	LYS12
B	LYS12
C	LYS12
D	LYS12

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:12403619, ECO:0000269|PubMed:19622869, ECO:0007744|PDB:1LYX, ECO:0007744|PDB:2VFI

Chain	Residue	Details
A	GLY171
B	GLY171
C	GLY171
D	GLY171

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:12454456, ECO:0000269|PubMed:14563846, ECO:0000269|PubMed:15465054, ECO:0000269|PubMed:19622869, ECO:0007744|PDB:1M7O, ECO:0007744|PDB:1O5X, ECO:0007744|PDB:1WOA, ECO:0007744|PDB:2VFI

Chain	Residue	Details
A	LEU230
B	LEU230
C	LEU230
D	LEU230

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:12403619, ECO:0000269|PubMed:12454456, ECO:0000269|PubMed:14563846, ECO:0000269|PubMed:15465054, ECO:0000269|PubMed:19622869, ECO:0000312|PDB:1LZO, ECO:0007744|PDB:1LYX, ECO:0007744|PDB:1M7O, ECO:0007744|PDB:1M7P, ECO:0007744|PDB:1O5X, ECO:0007744|PDB:1WOA, ECO:0007744|PDB:2VFI

Chain	Residue	Details
A	GLY232
B	GLY232
C	GLY232
D	GLY232

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	ASN10
A	HIS95
A	GLU165
A	GLY171
A	LYS12

---

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

Chain	Residue	Details
B	ASN10
B	HIS95
B	GLU165
B	GLY171
B	LYS12

---

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

Chain	Residue	Details
C	ASN10
C	HIS95
C	GLU165
C	GLY171
C	LYS12

---

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

Chain	Residue	Details
D	ASN10
D	HIS95
D	GLU165
D	GLY171
D	LYS12

---