Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1WOB

Structure of a loop6 hinge mutant of Plasmodium falciparum Triosephosphate Isomerase, W168F, complexed to sulfate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004807	molecular_function	triose-phosphate isomerase activity
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	0042802	molecular_function	identical protein binding
A	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
B	0004807	molecular_function	triose-phosphate isomerase activity
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	0042802	molecular_function	identical protein binding
B	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
C	0004807	molecular_function	triose-phosphate isomerase activity
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	0042802	molecular_function	identical protein binding
C	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
D	0004807	molecular_function	triose-phosphate isomerase activity
D	0005829	cellular_component	cytosol
D	0006094	biological_process	gluconeogenesis
D	0006096	biological_process	glycolytic process
D	0016853	molecular_function	isomerase activity
D	0019563	biological_process	glycerol catabolic process
D	0042802	molecular_function	identical protein binding
D	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 401

Chain	Residue
A	SER211
A	GLY232
A	ASN233
A	HOH429
A	HOH430

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 501

Chain	Residue
B	HOH525
B	SER211
B	GLY232
B	ASN233
B	HOH524

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 601

Chain	Residue
C	SER211
C	GLY232
C	ASN233
C	HOH622

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 701

Chain	Residue
C	HOH621
D	SER211
D	GLY232
D	ASN233
D	HOH735
D	HOH739

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)