Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6OOI

Crystal structure of triosephosphate isomerase from Schistosoma mansoni in complex with 2PG

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	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	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	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
D	0004807	molecular_function	triose-phosphate isomerase activity
D	0005737	cellular_component	cytoplasm
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	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	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
F	0004807	molecular_function	triose-phosphate isomerase activity
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006094	biological_process	gluconeogenesis
F	0006096	biological_process	glycolytic process
F	0016853	molecular_function	isomerase activity
F	0019563	biological_process	glycerol catabolic process
F	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	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
H	0004807	molecular_function	triose-phosphate isomerase activity
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0006094	biological_process	gluconeogenesis
H	0006096	biological_process	glycolytic process
H	0016853	molecular_function	isomerase activity
H	0019563	biological_process	glycerol catabolic process
H	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 A 301

Chain	Residue
A	LYS14
A	GLY236
A	GLY237
A	HOH434
A	HOH444
A	HOH448
A	HOH464
A	HIS96
A	GLU169
A	ALA173
A	ILE174
A	GLY175
A	GLY214
A	SER215
A	LEU234

site_id	AC2
Number of Residues	4
Details	binding site for residue CL A 302

Chain	Residue
A	ARG53
A	VAL62
A	ASP90
A	HOH450

site_id	AC3
Number of Residues	3
Details	binding site for residue NA A 303

Chain	Residue
A	LYS197
A	ALA200
A	ASN202

site_id	AC4
Number of Residues	3
Details	binding site for residue NA A 304

Chain	Residue
A	ARG53
A	LYS54
A	LEU56

site_id	AC5
Number of Residues	16
Details	binding site for residue PGA B 301

Chain	Residue
B	ASN12
B	LYS14
B	HIS96
B	GLU169
B	ALA173
B	ILE174
B	GLY175
B	GLY214
B	SER215
B	LEU234
B	GLY236
B	GLY237
B	HOH420
B	HOH432
B	HOH457
B	HOH465

site_id	AC6
Number of Residues	3
Details	binding site for residue CL B 302

Chain	Residue
B	ARG53
B	VAL62
B	ASP90

site_id	AC7
Number of Residues	3
Details	binding site for residue NA B 303

Chain	Residue
B	LYS197
B	ALA200
B	ASN202

site_id	AC8
Number of Residues	5
Details	binding site for residue GOL C 301

Chain	Residue
C	PHE103
C	HOH418
C	HOH512
D	PHE103
D	HOH454

site_id	AC9
Number of Residues	16
Details	binding site for residue PGA C 302

Chain	Residue
C	ASN12
C	LYS14
C	HIS96
C	GLU169
C	ALA173
C	ILE174
C	GLY175
C	GLY214
C	SER215
C	LEU234
C	GLY236
C	GLY237
C	HOH407
C	HOH424
C	HOH445
C	HOH486

site_id	AD1
Number of Residues	3
Details	binding site for residue CL C 303

Chain	Residue
C	ARG53
C	VAL62
C	ASP90

site_id	AD2
Number of Residues	3
Details	binding site for residue NA C 304

Chain	Residue
C	ARG53
C	LYS54
C	LEU56

site_id	AD3
Number of Residues	5
Details	binding site for residue NA C 305

Chain	Residue
C	ALA225
C	GLN227
C	HIS228
C	VAL230
C	ARG251

site_id	AD4
Number of Residues	15
Details	binding site for residue PGA D 301

Chain	Residue
D	LYS14
D	HIS96
D	GLU169
D	ALA173
D	ILE174
D	GLY175
D	GLY214
D	SER215
D	LEU234
D	GLY236
D	GLY237
D	HOH406
D	HOH419
D	HOH435
D	HOH440

site_id	AD5
Number of Residues	3
Details	binding site for residue CL D 302

Chain	Residue
D	ARG53
D	VAL62
D	ASP90

site_id	AD6
Number of Residues	12
Details	binding site for residue PGA E 301

Chain	Residue
E	HIS96
E	GLU169
E	ILE174
E	GLY175
E	SER215
E	GLY236
E	GLY237
E	HOH406
E	HOH421
E	HOH457
E	ASN12
E	LYS14

site_id	AD7
Number of Residues	4
Details	binding site for residue NA E 302

Chain	Residue
E	ALA225
E	GLN227
E	HIS228
E	VAL230

site_id	AD8
Number of Residues	3
Details	binding site for residue NA E 303

Chain	Residue
E	ARG53
E	LYS54
E	LEU56

site_id	AD9
Number of Residues	15
Details	binding site for residue PGA F 301

Chain	Residue
F	LYS14
F	HIS96
F	GLU169
F	ALA173
F	ILE174
F	GLY175
F	GLY214
F	SER215
F	LEU234
F	GLY236
F	GLY237
F	HOH433
F	HOH445
F	HOH468
F	HOH490

site_id	AE1
Number of Residues	3
Details	binding site for residue CL F 302

Chain	Residue
F	ARG53
F	VAL62
F	ASP90

site_id	AE2
Number of Residues	16
Details	binding site for residue PGA G 301

Chain	Residue
G	ASN12
G	LYS14
G	HIS96
G	GLU169
G	ALA173
G	ILE174
G	GLY175
G	GLY214
G	SER215
G	LEU234
G	GLY236
G	GLY237
G	HOH410
G	HOH427
G	HOH438
G	HOH447

site_id	AE3
Number of Residues	4
Details	binding site for residue CL G 302

Chain	Residue
D	HOH421
G	ARG53
G	VAL62
G	ASP90

site_id	AE4
Number of Residues	4
Details	binding site for residue GOL H 301

Chain	Residue
G	PHE103
G	HOH415
H	PHE103
H	GLY104

site_id	AE5
Number of Residues	14
Details	binding site for residue PGA H 302

Chain	Residue
H	LYS14
H	HIS96
H	GLU169
H	ALA173
H	ILE174
H	GLY175
H	GLY214
H	SER215
H	LEU234
H	GLY236
H	GLY237
H	HOH431
H	HOH451
H	HOH457

site_id	AE6
Number of Residues	3
Details	binding site for residue NA H 303

Chain	Residue
H	ARG53
H	LYS54
H	LEU56

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ALA167-GLY177

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Electrophile","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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