Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3IDS

Structure of Glycosomal Glyceraldehyde-3-Phosphate Dehydrogenase from Trypanosoma cruzi in complex with the irreversible iodoacetamide inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
A	0005829	cellular_component	cytosol
A	0006006	biological_process	glucose metabolic process
A	0006096	biological_process	glycolytic process
A	0016491	molecular_function	oxidoreductase activity
A	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A	0020015	cellular_component	glycosome
A	0050661	molecular_function	NADP binding
A	0051287	molecular_function	NAD binding
B	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
B	0005829	cellular_component	cytosol
B	0006006	biological_process	glucose metabolic process
B	0006096	biological_process	glycolytic process
B	0016491	molecular_function	oxidoreductase activity
B	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B	0020015	cellular_component	glycosome
B	0050661	molecular_function	NADP binding
B	0051287	molecular_function	NAD binding
C	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
C	0005829	cellular_component	cytosol
C	0006006	biological_process	glucose metabolic process
C	0006096	biological_process	glycolytic process
C	0016491	molecular_function	oxidoreductase activity
C	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C	0020015	cellular_component	glycosome
C	0050661	molecular_function	NADP binding
C	0051287	molecular_function	NAD binding
D	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
D	0005829	cellular_component	cytosol
D	0006006	biological_process	glucose metabolic process
D	0006096	biological_process	glycolytic process
D	0016491	molecular_function	oxidoreductase activity
D	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D	0020015	cellular_component	glycosome
D	0050661	molecular_function	NADP binding
D	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACM C 360

Chain	Residue
C	SER165
C	CYS166
C	ASN335
C	TYR339
C	HOH545
C	HOH716

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 361

Chain	Residue
C	HOH389
C	HOH412
C	HOH533
C	LEU296
C	ASP300
C	ASP304

site_id	AC3
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAD D 360

Chain	Residue
D	GLY9
D	GLY11
D	ARG12
D	ILE13
D	VAL37
D	ASP38
D	MET39
D	ALA90
D	GLN91
D	SER110
D	THR111
D	GLY112
D	LEU113
D	SER134
D	ALA135
D	CYS166
D	ALA198
D	ASN335
D	TYR339
D	HOH384
D	HOH394
D	HOH395
D	HOH412
D	HOH436
D	HOH569
D	HOH860
D	HOH883

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 361

Chain	Residue
D	TYR291
D	THR292
D	ASP293
D	HOH397
D	HOH490
D	HOH1084

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D 362

Chain	Residue
D	VAL104
D	GLY127
D	ARG129
D	HOH663
D	HOH1164

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACM A 360

Chain	Residue
A	CYS166
A	ASN335
A	HOH432
A	HOH511
A	HOH512

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 361

Chain	Residue
A	ASP300
A	ASP304
A	HOH459
A	HOH462
A	HOH499
C	LYS58

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 362

Chain	Residue
A	ASP24
A	GLY25
A	GLU30

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACM B 360

Chain	Residue
B	SER165
B	CYS166
B	ASN335
B	HOH706
B	HOH873

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 361

Chain	Residue
B	TYR291
B	THR292
B	ASP293
B	HOH424
B	HOH467
B	HOH587

Functional Information from PROSITE/UniProt

site_id	PS00071
Number of Residues	8
Details	GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL

Chain	Residue	Details
C	ALA164-LEU171

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Motif: {"description":"Microbody targeting signal","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Nucleophile"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12795610","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14622286","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	20
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Site: {"description":"Activates thiol group during catalysis"}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1szj

Chain	Residue	Details
C	CYS166
C	HIS194

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1szj

Chain	Residue	Details
D	CYS166
D	HIS194

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1szj

Chain	Residue	Details
A	CYS166
A	HIS194

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1szj

Chain	Residue	Details
B	CYS166
B	HIS194

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