Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1NPT

Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 replaced by Ala 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	8
Details	BINDING SITE FOR RESIDUE SO4 O 1338

Chain	Residue
O	THR179
O	ASP181
O	ARG195
O	ARG231
O	NAD1336
O	HOH1353
O	HOH1563
O	HOH1602

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 P 2338

Chain	Residue
P	ASP181
P	ARG195
P	ARG231
P	NAD2336
P	HOH2353
P	HOH2524
P	THR179

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 Q 3338

Chain	Residue
Q	THR179
Q	ASP181
Q	ARG195
Q	ARG231
Q	NAD3336
Q	HOH3547

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 R 4338

Chain	Residue
R	THR179
R	ASP181
R	ARG195
R	ARG231
R	NAD4336
R	HOH4353
R	HOH4440
R	HOH4485
R	HOH4514
R	HOH4610

site_id	AC5
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NAD O 1336

Chain	Residue
O	GLY7
O	GLY9
O	ARG10
O	ILE11
O	ASN31
O	ASP32
O	LEU33
O	ARG77
O	SER95
O	THR96
O	GLY97
O	SER119
O	ALA120
O	ASN180
O	ASN313
O	TYR317
O	SO41338
O	HOH1353
O	HOH1354
O	HOH1356
O	HOH1367
O	HOH1380
O	HOH1388
O	HOH1478
O	HOH1539
O	HOH1576
O	HOH1577
O	HOH1595
O	HOH1610
O	HOH4505
O	HOH4507

site_id	AC6
Number of Residues	34
Details	BINDING SITE FOR RESIDUE NAD P 2336

Chain	Residue
P	GLY7
P	PHE8
P	GLY9
P	ARG10
P	ILE11
P	ASN31
P	ASP32
P	GLU76
P	ARG77
P	SER95
P	THR96
P	GLY97
P	SER119
P	ALA120
P	ASN180
P	ASN313
P	TYR317
P	SO42338
P	HOH2353
P	HOH2354
P	HOH2356
P	HOH2366
P	HOH2367
P	HOH2380
P	HOH2388
P	HOH2416
P	HOH2478
P	HOH2561
P	HOH2582
P	HOH2583
P	HOH2603
P	HOH2604
Q	LEU187
Q	HOH2373

site_id	AC7
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NAD Q 3336

Chain	Residue
Q	ARG10
Q	ILE11
Q	ASN31
Q	ASP32
Q	ARG77
Q	SER95
Q	THR96
Q	GLY97
Q	PHE99
Q	SER119
Q	ALA120
Q	ASN180
Q	ASN313
Q	TYR317
Q	HOH2508
Q	HOH2519
Q	HOH2637
Q	SO43338
Q	HOH3354
Q	HOH3356
Q	HOH3367
Q	HOH3373
Q	HOH3380
Q	HOH3388
Q	HOH3415
Q	HOH3430
Q	HOH3546
Q	HOH3547
P	LEU187
Q	GLY7
Q	GLY9

site_id	AC8
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NAD R 4336

Chain	Residue
O	HOH4373
R	GLY7
R	GLY9
R	ARG10
R	ILE11
R	ASN31
R	ASP32
R	LEU33
R	ARG77
R	SER95
R	THR96
R	GLY97
R	SER119
R	ALA120
R	ASN180
R	ASN313
R	TYR317
R	SO44338
R	HOH4353
R	HOH4354
R	HOH4356
R	HOH4366
R	HOH4367
R	HOH4380
R	HOH4388
R	HOH4390
R	HOH4415
R	HOH4416
R	HOH4430
R	HOH4478
R	HOH4610

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	ALA149
R	ALA149
R	ASN180
R	VAL232
O	ASN180
O	VAL232
P	ALA149
P	ASN180
P	VAL232
Q	ALA149
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	ALA149
O	HIS176

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

Chain	Residue	Details
P	ALA149
P	HIS176

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

Chain	Residue	Details
Q	ALA149
Q	HIS176

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

Chain	Residue	Details
R	ALA149
R	HIS176

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