Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1DBV

GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE MUTANT WITH ASP 32 REPLACED BY GLY, LEU 187 REPLACED BY ALA, AND PRO 188 REPLACED BY SER COMPLEXED WITH NAD+

Functional Information from GO Data

Chain	GOid	namespace	contents
O	0000166	molecular_function	nucleotide binding
O	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
O	0005737	cellular_component	cytoplasm
O	0006006	biological_process	glucose metabolic process
O	0006096	biological_process	glycolytic process
O	0016491	molecular_function	oxidoreductase activity
O	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
O	0030554	molecular_function	adenyl nucleotide binding
O	0050661	molecular_function	NADP binding
O	0051287	molecular_function	NAD binding
P	0000166	molecular_function	nucleotide binding
P	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
P	0005737	cellular_component	cytoplasm
P	0006006	biological_process	glucose metabolic process
P	0006096	biological_process	glycolytic process
P	0016491	molecular_function	oxidoreductase activity
P	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
P	0030554	molecular_function	adenyl nucleotide binding
P	0050661	molecular_function	NADP binding
P	0051287	molecular_function	NAD binding
Q	0000166	molecular_function	nucleotide binding
Q	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
Q	0005737	cellular_component	cytoplasm
Q	0006006	biological_process	glucose metabolic process
Q	0006096	biological_process	glycolytic process
Q	0016491	molecular_function	oxidoreductase activity
Q	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Q	0030554	molecular_function	adenyl nucleotide binding
Q	0050661	molecular_function	NADP binding
Q	0051287	molecular_function	NAD binding
R	0000166	molecular_function	nucleotide binding
R	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
R	0005737	cellular_component	cytoplasm
R	0006006	biological_process	glucose metabolic process
R	0006096	biological_process	glycolytic process
R	0016491	molecular_function	oxidoreductase activity
R	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
R	0030554	molecular_function	adenyl nucleotide binding
R	0050661	molecular_function	NADP binding
R	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 O 338

Chain	Residue
O	THR179
O	ASP181
O	ARG195
O	ARG231
O	NAD336
O	HOH344

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 O 339

Chain	Residue
O	ALA210
O	HOH380
O	HOH409
O	SER148
O	THR208
O	GLY209

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 P 338

Chain	Residue
P	THR179
P	ASP181
P	ARG195
P	ARG231
P	NAD336
P	HOH352
P	HOH410

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 P 339

Chain	Residue
P	SER148
P	THR208
P	GLY209
P	ALA210
P	HOH388
P	HOH409
P	HOH423

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 Q 338

Chain	Residue
Q	THR179
Q	ASP181
Q	ARG195
Q	ARG231
Q	NAD336
Q	HOH355

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 Q 339

Chain	Residue
Q	SER148
Q	THR208
Q	GLY209
Q	ALA210
Q	HOH353
Q	HOH391
Q	HOH411
Q	HOH418
Q	HOH437

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 R 338

Chain	Residue
R	THR179
R	ASP181
R	ARG195
R	ARG231
R	NAD336

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 R 339

Chain	Residue
R	SER148
R	THR208
R	GLY209
R	ALA210
R	HOH390
R	HOH402
R	HOH425

site_id	AC9
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAD O 336

Chain	Residue
O	GLY9
O	ARG10
O	ILE11
O	ASN31
O	LEU33
O	GLU76
O	ARG77
O	SER95
O	THR96
O	GLY97
O	SER119
O	ALA120
O	CYS149
O	ASN180
O	ASN313
O	TYR317
O	SO4338
O	HOH344
O	HOH345
O	HOH347
O	HOH357
O	HOH364
O	HOH370
O	HOH373
O	HOH374
O	HOH425
O	HOH426

site_id	BC1
Number of Residues	28
Details	BINDING SITE FOR RESIDUE NAD P 336

Chain	Residue
P	HOH353
P	HOH355
P	HOH364
P	HOH365
P	HOH380
P	HOH382
P	HOH415
P	HOH425
Q	HOH342
P	GLY7
P	GLY9
P	ARG10
P	ILE11
P	ASN31
P	LEU33
P	ARG77
P	SER95
P	THR96
P	GLY97
P	ARG98
P	PHE99
P	SER119
P	ALA120
P	ASN180
P	ASN313
P	TYR317
P	SO4338
P	HOH352

site_id	BC2
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAD Q 336

Chain	Residue
P	HOH426
Q	GLY7
Q	GLY9
Q	ARG10
Q	ILE11
Q	LEU33
Q	GLU76
Q	ARG77
Q	SER95
Q	THR96
Q	GLY97
Q	SER119
Q	ALA120
Q	CYS149
Q	ASN180
Q	ASN313
Q	TYR317
Q	SO4338
Q	HOH355
Q	HOH356
Q	HOH366
Q	HOH379
Q	HOH382
Q	HOH383
Q	HOH397
Q	HOH438
Q	HOH439

site_id	BC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAD R 336

Chain	Residue
O	HOH437
R	GLY7
R	PHE8
R	GLY9
R	ARG10
R	ILE11
R	LEU33
R	ARG77
R	SER95
R	THR96
R	GLY97
R	ARG98
R	SER119
R	ALA120
R	CYS149
R	ASN180
R	ASN313
R	TYR317
R	SO4338
R	HOH352
R	HOH361
R	HOH370
R	HOH427

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
O	ALA147-LEU154

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Nucleophile => ECO:0000269\|PubMed:18480053, ECO:0000305\|PubMed:12569100

Chain	Residue	Details
O	THR150
P	THR150
Q	THR150
R	THR150

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:12569100, ECO:0000269\|PubMed:18480053, ECO:0000269\|PubMed:3586018, ECO:0000269\|PubMed:9175858

Chain	Residue	Details
O	ILE11
P	ALA120
P	ASP181
P	GLU314
Q	ILE11
Q	LEU33
Q	ASP78
Q	ALA120
Q	ASP181
Q	GLU314
R	ILE11
O	LEU33
R	LEU33
R	ASP78
R	ALA120
R	ASP181
R	GLU314
O	ASP78
O	ALA120
O	ASP181
O	GLU314
P	ILE11
P	LEU33
P	ASP78

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:12569100, ECO:0000269\|PubMed:18480053, ECO:0000269\|PubMed:3210237, ECO:0000269\|PubMed:3586018, ECO:0000269\|PubMed:9175858

Chain	Residue	Details
O	CYS149
R	CYS149
R	ASN180
R	VAL232
O	ASN180
O	VAL232
P	CYS149
P	ASN180
P	VAL232
Q	CYS149
Q	ASN180
Q	VAL232

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:12569100, ECO:0000269\|PubMed:18480053, ECO:0000269\|PubMed:9175858

Chain	Residue	Details
O	ALA196
P	ALA196
Q	ALA196
R	ALA196

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:18480053, ECO:0000269\|PubMed:3210237, ECO:0000269\|PubMed:3586018, ECO:0000269\|PubMed:9175858

Chain	Residue	Details
O	GLY209
P	GLY209
Q	GLY209
R	GLY209

site_id	SWS_FT_FI6
Number of Residues	4
Details	SITE: Activates thiol group during catalysis => ECO:0000250\|UniProtKB:Q6GIL8

Chain	Residue	Details
O	SER177
P	SER177
Q	SER177
R	SER177

Catalytic Information from CSA

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

Chain	Residue	Details
O	CYS149
O	HIS176

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

Chain	Residue	Details
P	CYS149
P	HIS176

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

Chain	Residue	Details
Q	CYS149
Q	HIS176

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

Chain	Residue	Details
R	CYS149
R	HIS176

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