Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3DBV

GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE MUTANT WITH LEU 33 REPLACED BY THR, THR 34 REPLACED BY GLY, ASP 36 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	HOH387

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

Chain	Residue
O	GLY209
O	ALA210
O	HOH385
O	SER148
O	THR150
O	THR208

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 P 338

Chain	Residue
P	THR179
P	ARG195
P	ARG231
P	NAD336
P	HOH344
P	HOH393

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 P 339

Chain	Residue
P	SER148
P	THR208
P	GLY209
P	ALA210
P	HOH372

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	HOH343

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 Q 339

Chain	Residue
Q	SER148
Q	THR208
Q	GLY209
Q	ALA210
Q	HOH401

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	5
Details	BINDING SITE FOR RESIDUE SO4 R 339

Chain	Residue
R	SER148
R	THR150
R	THR208
R	ALA210
R	HOH380

site_id	AC9
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NAD O 336

Chain	Residue
O	GLY9
O	ARG10
O	ILE11
O	ASP32
O	THR33
O	GLU76
O	ARG77
O	SER95
O	GLY97
O	SER119
O	ALA120
O	CYS149
O	ASN180
O	ASN313
O	SO4338
O	HOH344
O	HOH357
O	HOH362
O	HOH364
O	HOH366
O	HOH403

site_id	BC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAD P 336

Chain	Residue
P	GLY7
P	GLY9
P	ARG10
P	ILE11
P	ASN31
P	ASP32
P	GLU76
P	ARG77
P	SER95
P	THR96
P	GLY97
P	ARG98
P	PHE99
P	SER119
P	ALA120
P	ASN180
P	ASN313
P	SO4338
P	HOH344
P	HOH347
P	HOH353
P	HOH357
P	HOH361
P	HOH365
P	HOH393

site_id	BC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAD Q 336

Chain	Residue
Q	SER95
Q	THR96
Q	GLY97
Q	ARG98
Q	SER119
Q	ALA120
Q	ASN313
Q	TYR317
Q	SO4338
Q	HOH343
Q	HOH344
Q	HOH353
Q	HOH354
Q	HOH363
Q	HOH368
P	HOH411
Q	GLY7
Q	PHE8
Q	GLY9
Q	ARG10
Q	ILE11
Q	ASP32
Q	THR33
Q	ARG77

site_id	BC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NAD R 336

Chain	Residue
R	GLY7
R	PHE8
R	GLY9
R	ARG10
R	ILE11
R	ASN31
R	ASP32
R	THR33
R	ARG77
R	SER95
R	THR96
R	GLY97
R	SER119
R	ALA120
R	ASN180
R	ASN313
R	TYR317
R	SO4338
R	HOH359
R	HOH367
R	HOH370

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	THR33
Q	ASP78
Q	ALA120
Q	ASP181
Q	GLU314
R	ILE11
O	THR33
R	THR33
R	ASP78
R	ALA120
R	ASP181
R	GLU314
O	ASP78
O	ALA120
O	ASP181
O	GLU314
P	ILE11
P	THR33
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)