Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1I32

LEISHMANIA MEXICANA GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE IN COMPLEX WITH INHIBITORS

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE NMD A 361

Chain	Residue
A	ASN8
A	ARG92
A	THR111
A	LEU113
A	HOH992
B	VAL206
A	GLY9
A	GLY11
A	VAL37
A	ASP38
A	MET39
A	SER40
A	ALA90
A	GLN91

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE NMD B 362

Chain	Residue
A	VAL206
B	ASN8
B	GLY9
B	GLY11
B	VAL37
B	ASP38
B	MET39
B	SER40
B	ALA90
B	GLN91
B	ARG92
B	THR111
B	LEU113
B	HOH551
B	HOH890
B	HOH1006

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE NMD C 363

Chain	Residue
C	ASN8
C	GLY9
C	GLY11
C	VAL37
C	ASP38
C	MET39
C	SER40
C	ALA90
C	GLN91
C	ARG92
C	THR111
C	HOH515
C	HOH554
D	LEU208

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE NMD D 364

Chain	Residue
C	LEU208
D	ASN8
D	GLY9
D	GLY11
D	ASP38
D	MET39
D	SER40
D	ALA90
D	GLN91
D	ARG92
D	THR111
D	LEU113
D	HOH1065
D	HOH1157

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE NMD E 365

Chain	Residue
E	ASN8
E	GLY9
E	GLY11
E	ASP38
E	MET39
E	SER40
E	ALA90
E	GLN91
E	ARG92
E	THR111
E	LEU113
E	HOH599
F	VAL206

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE NMD F 366

Chain	Residue
E	VAL206
F	ASN8
F	GLY9
F	GLY11
F	ASP38
F	MET39
F	SER40
F	ALA90
F	GLN91
F	SER110
F	THR111
F	LEU113
F	HOH651
F	HOH980

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ALA164-LEU171

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Nucleophile"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7578111","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9571030","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	30
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
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
A	CYS166
A	HIS194

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

Chain	Residue	Details
B	CYS166
B	HIS194

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

Chain	Residue	Details
C	CYS166
C	HIS194

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

Chain	Residue	Details
D	CYS166
D	HIS194

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1szj

Chain	Residue	Details
E	CYS166
E	HIS194

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1szj

Chain	Residue	Details
F	CYS166
F	HIS194

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)