1NQO

Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 Replaced By Ser Complexed With Nad+ and D-Glyceraldehyde-3-Phosphate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
A	0005737	cellular_component	cytoplasm
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	0030554	molecular_function	adenyl nucleotide binding
A	0050661	molecular_function	NADP binding
A	0051287	molecular_function	NAD binding
C	0000166	molecular_function	nucleotide binding
C	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
C	0005737	cellular_component	cytoplasm
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	0030554	molecular_function	adenyl nucleotide binding
C	0050661	molecular_function	NADP binding
C	0051287	molecular_function	NAD binding
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
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	33
Details	BINDING SITE FOR RESIDUE NAD O 1336

Chain	Residue
O	GLY7
O	SER95
O	THR96
O	GLY97
O	SER119
O	ALA120
O	ASN180
O	ASN313
O	TYR317
O	G3H1337
O	HOH1341
O	PHE8
O	HOH1353
O	HOH1360
O	HOH1364
O	HOH1366
O	HOH1369
O	HOH1394
O	HOH1468
O	HOH1477
O	HOH1479
O	HOH1499
O	GLY9
O	HOH1621
Q	LEU187
Q	HOH3437
Q	HOH3513
O	ARG10
O	ILE11
O	ASN31
O	ASP32
O	GLU76
O	ARG77

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE G3H O 1337

Chain	Residue
O	SER148
O	SER149
O	THR150
O	HIS176
O	THR179
O	ARG195
O	ARG231
O	NAD1336
O	HOH1353
O	HOH1621

---

site_id	AC3
Number of Residues	32
Details	BINDING SITE FOR RESIDUE NAD Q 3336

Chain	Residue
O	LEU187
O	HOH1402
O	HOH1486
Q	GLY7
Q	GLY9
Q	ARG10
Q	ILE11
Q	ASN31
Q	ASP32
Q	LEU33
Q	GLU76
Q	ARG77
Q	SER95
Q	THR96
Q	GLY97
Q	PHE99
Q	SER119
Q	ALA120
Q	ASN180
Q	ASN313
Q	TYR317
Q	HOH1495
Q	HOH1497
Q	G3H3337
Q	HOH3342
Q	HOH3353
Q	HOH3377
Q	HOH3389
Q	HOH3390
Q	HOH3430
Q	HOH3489
Q	HOH3502

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE G3H Q 3337

Chain	Residue
Q	SER149
Q	THR150
Q	HIS176
Q	THR179
Q	ARG195
Q	ARG231
Q	NAD3336
Q	HOH3353
Q	HOH3421
Q	HOH3621

---

site_id	AC5
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NAD A 5336

Chain	Residue
A	SER119
A	ALA120
A	ASN180
A	LEU187
A	ASN313
A	TYR317
A	G3H5337
A	HOH5341
A	HOH5353
A	HOH5369
A	HOH5377
A	HOH5411
A	HOH5475
A	HOH5487
A	HOH5492
A	HOH5510
A	HOH5621
A	GLY7
A	PHE8
A	GLY9
A	ARG10
A	ILE11
A	ASN31
A	ASP32
A	LEU33
A	GLU76
A	ARG77
A	SER95
A	THR96
A	GLY97
A	PHE99

---

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE G3H A 5337

Chain	Residue
A	SER149
A	THR150
A	HIS176
A	THR179
A	ASP181
A	ARG195
A	ARG231
A	NAD5336
A	HOH5353
A	HOH5405
A	HOH5621

---

site_id	AC7
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NAD C 7336

Chain	Residue
C	GLY7
C	GLY9
C	ARG10
C	ILE11
C	ASN31
C	ASP32
C	LEU33
C	GLU76
C	ARG77
C	SER95
C	THR96
C	GLY97
C	SER119
C	ALA120
C	ASN180
C	LEU187
C	ASN313
C	TYR317
C	G3H7337
C	HOH7342
C	HOH7353
C	HOH7366
C	HOH7373
C	HOH7374
C	HOH7405
C	HOH7412
C	HOH7474
C	HOH7482
C	HOH7491
C	HOH7499
C	HOH7501

---

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE G3H C 7337

Chain	Residue
C	SER149
C	THR150
C	HIS176
C	THR179
C	ASP181
C	ARG231
C	NAD7336
C	HOH7353
C	HOH7621

---

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
Q	THR150
A	THR150
C	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
Q	ALA120
Q	ASP181
Q	GLU314
A	ILE11
A	LEU33
A	ASP78
A	ALA120
A	ASP181
A	GLU314
C	ILE11
O	LEU33
C	LEU33
C	ASP78
C	ALA120
C	ASP181
C	GLU314
O	ASP78
O	ALA120
O	ASP181
O	GLU314
Q	ILE11
Q	LEU33
Q	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	SER149
C	SER149
C	ASN180
C	VAL232
O	ASN180
O	VAL232
Q	SER149
Q	ASN180
Q	VAL232
A	SER149
A	ASN180
A	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
Q	ALA196
A	ALA196
C	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
Q	GLY209
A	GLY209
C	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
Q	SER177
A	SER177
C	SER177

---

Catalytic Information from CSA

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

Chain	Residue	Details
O	SER149
O	HIS176

---

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

Chain	Residue	Details
Q	SER149
Q	HIS176

---

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

Chain	Residue	Details
A	SER149
A	HIS176

---

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

Chain	Residue	Details
C	SER149
C	HIS176

---