2DBV

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

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	5
Details	BINDING SITE FOR RESIDUE SO4 O 338

Chain	Residue
O	THR179
O	ARG195
O	ARG231
O	NDP336
O	HOH400

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 O 339

Chain	Residue
O	HOH399
O	SER148
O	THR208
O	GLY209
O	ALA210

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 P 338

Chain	Residue
P	THR179
P	ASP181
P	ARG195
P	ARG231
P	NDP336
P	HOH351
P	HOH400
P	HOH408
P	HOH411

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 P 339

Chain	Residue
P	SER148
P	THR208
P	GLY209
P	ALA210
P	HOH349
P	HOH387
P	HOH424
P	HOH427

---

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

Chain	Residue
Q	THR179
Q	ASP181
Q	ARG231
Q	NDP336
Q	HOH349
Q	HOH396

---

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	HOH418

---

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 R 338

Chain	Residue
R	THR179
R	ASP181
R	ARG195
R	ARG231
R	NDP336
R	HOH356
R	HOH405

---

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	HOH354
R	HOH387
R	HOH427

---

site_id	AC9
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NDP O 336

Chain	Residue
O	ASN6
O	GLY7
O	GLY9
O	ARG10
O	ILE11
O	ASN31
O	GLY32
O	LEU33
O	ARG77
O	SER95
O	THR96
O	GLY97
O	SER119
O	ALA120
O	CYS149
O	ASN180
O	ASN313
O	TYR317
O	SO4338
O	HOH347
O	HOH355
O	HOH356
O	HOH362
O	HOH368
O	HOH370
O	HOH371
O	HOH422
O	HOH423
O	HOH424
R	SER188

---

site_id	BC1
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NDP P 336

Chain	Residue
P	GLU314
P	SO4338
P	HOH351
P	HOH352
P	HOH353
P	HOH360
P	HOH365
P	HOH371
P	HOH376
P	HOH390
P	HOH435
Q	SER188
Q	HOH343
P	GLY9
P	ARG10
P	ILE11
P	ASN31
P	LEU33
P	GLU76
P	ARG77
P	SER95
P	THR96
P	GLY97
P	ARG98
P	PHE99
P	SER119
P	ALA120
P	CYS149
P	ASN180
P	ASN313

---

site_id	BC2
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NDP Q 336

Chain	Residue
P	SER188
Q	PHE8
Q	GLY9
Q	ARG10
Q	ILE11
Q	ASN31
Q	LEU33
Q	ARG77
Q	SER95
Q	THR96
Q	GLY97
Q	SER119
Q	ALA120
Q	ASN180
Q	ASN313
Q	TYR317
Q	SO4338
Q	HOH350
Q	HOH361
Q	HOH362
Q	HOH365
Q	HOH371
Q	HOH375
Q	HOH421
Q	HOH422
Q	HOH423

---

site_id	BC3
Number of Residues	29
Details	BINDING SITE FOR RESIDUE NDP R 336

Chain	Residue
O	SER188
R	GLY7
R	PHE8
R	GLY9
R	ARG10
R	ILE11
R	ASN31
R	GLY32
R	LEU33
R	ARG77
R	SER95
R	THR96
R	GLY97
R	SER119
R	ALA120
R	CYS149
R	ASN180
R	ASN313
R	TYR317
R	SO4338
R	HOH356
R	HOH357
R	HOH366
R	HOH367
R	HOH375
R	HOH381
R	HOH432
R	HOH433
R	HOH434

---

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	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"18480053","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12569100","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12569100","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18480053","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3586018","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9175858","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12569100","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18480053","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3210237","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3586018","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9175858","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12569100","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18480053","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9175858","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18480053","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3210237","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3586018","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9175858","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Site: {"description":"Activates thiol group during catalysis","evidences":[{"source":"UniProtKB","id":"Q6GIL8","evidenceCode":"ECO:0000250"}]}

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
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

---