Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1A7K

GLYCOSOMAL GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE IN A MONOCLINIC CRYSTAL FORM

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	8
Details	BINDING SITE FOR RESIDUE PO4 A 361

Chain	Residue
A	SER165
A	CYS166
A	THR167
A	HIS194
A	THR225
A	THR226
A	GLY227
A	ALA228

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 362

Chain	Residue
A	THR199
A	ARG249
A	NAD363
A	THR197

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 B 361

Chain	Residue
B	SER165
B	CYS166
B	THR167
B	HIS194
B	THR226
B	GLY227
B	ALA228

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 B 362

Chain	Residue
B	THR197
B	THR199
B	NAD363

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 C 361

Chain	Residue
C	SER165
C	CYS166
C	THR167
C	HIS194
C	THR226
C	GLY227
C	ALA228

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 C 362

Chain	Residue
C	THR197
C	THR199
C	ARG249
C	NAD363

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 D 361

Chain	Residue
D	SER165
D	CYS166
D	THR167
D	THR226
D	GLY227
D	ALA228

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 D 362

Chain	Residue
D	THR197
D	THR199
D	ARG249
D	NAD363

site_id	AC9
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAD A 363

Chain	Residue
A	ASN8
A	GLY9
A	GLY11
A	ARG12
A	ILE13
A	VAL37
A	ASP38
A	MET39
A	ALA90
A	GLN91
A	SER110
A	THR111
A	GLY112
A	LEU113
A	SER134
A	ALA135
A	CYS166
A	THR197
A	ALA198
A	ASN335
A	GLU336
A	TYR339
A	PO4362

site_id	BC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE NAD B 363

Chain	Residue
B	ASN8
B	GLY9
B	GLY11
B	ARG12
B	ILE13
B	VAL37
B	ASP38
B	MET39
B	ALA90
B	SER110
B	THR111
B	LEU113
B	SER134
B	ALA135
B	CYS166
B	ASN335
B	PO4362

site_id	BC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NAD C 363

Chain	Residue
C	TYR339
C	PO4362
D	VAL206
C	ASN8
C	GLY9
C	PHE10
C	GLY11
C	ARG12
C	ILE13
C	VAL37
C	ASP38
C	GLN91
C	SER110
C	THR111
C	GLY112
C	LEU113
C	SER134
C	CYS166
C	ASN335

site_id	BC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NAD D 363

Chain	Residue
D	ASN8
D	GLY9
D	GLY11
D	ARG12
D	ILE13
D	VAL37
D	ASP38
D	MET39
D	ALA90
D	GLN91
D	THR111
D	GLY112
D	LEU113
D	SER134
D	ALA135
D	CYS166
D	ALA198
D	ASN335
D	GLU336
D	TYR339
D	PO4362

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	4
Details	Active site: {"description":"Nucleophile"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	20
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	20
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
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
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

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