1GAE

COMPARISON OF THE STRUCTURES OF WILD TYPE AND A N313T MUTANT OF ESCHERICHIA COLI GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASES: IMPLICATION FOR NAD BINDING AND COOPERATIVITY

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	0005515	molecular_function	protein binding
O	0005737	cellular_component	cytoplasm
O	0005829	cellular_component	cytosol
O	0006006	biological_process	glucose metabolic process
O	0006096	biological_process	glycolytic process
O	0016020	cellular_component	membrane
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	0042802	molecular_function	identical protein 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	0005515	molecular_function	protein binding
P	0005737	cellular_component	cytoplasm
P	0005829	cellular_component	cytosol
P	0006006	biological_process	glucose metabolic process
P	0006096	biological_process	glycolytic process
P	0016020	cellular_component	membrane
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	0042802	molecular_function	identical protein binding
P	0050661	molecular_function	NADP binding
P	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE NAD O 336

Chain	Residue
O	GLY7
O	THR96
O	GLY97
O	THR119
O	CYS149
O	THR313
O	HOH344
O	HOH351
O	HOH452
O	PHE8
O	GLY9
O	ARG10
O	ILE11
O	ASN31
O	ASP32
O	GLU76
O	ALA95

---

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE NAD P 336

Chain	Residue
P	GLY7
P	PHE8
P	GLY9
P	ARG10
P	ILE11
P	ASP32
P	ARG77
P	ALA95
P	THR96
P	GLY97
P	LEU98
P	THR119
P	CYS149
P	THR313
P	HOH350
P	HOH356

---

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	2
Details	ACT_SITE: Nucleophile => ECO:0000305|PubMed:10978154

Chain	Residue	Details
O	THR150
P	THR150

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984, ECO:0000269|Ref.18

Chain	Residue	Details
O	ILE11
P	ILE11

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984

Chain	Residue	Details
O	LEU33
O	GLU314
P	LEU33
P	GLU314

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219

Chain	Residue	Details
O	ASP78
P	ASP78

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:19542219

Chain	Residue	Details
O	GLY120
P	GLY120

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:10978154

Chain	Residue	Details
O	CYS149
O	GLY209
P	CYS149
P	GLY209

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P00362

Chain	Residue	Details
O	ALA180
P	ALA180

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:19542219, ECO:0000269|Ref.18, ECO:0000305|PubMed:10978154

Chain	Residue	Details
O	VAL232
P	VAL232

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	SITE: Activates thiol group during catalysis => ECO:0000269|PubMed:2659073

Chain	Residue	Details
O	ALA177
P	ALA177

---

site_id	SWS_FT_FI10
Number of Residues	16
Details	MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122

Chain	Residue	Details
O	LYS115
P	ASP123
P	ALA213
P	VAL217
P	LEU225
P	ALA249
P	ALA257
P	ALA261
O	ASP123
O	ALA213
O	VAL217
O	LEU225
O	ALA249
O	ALA257
O	ALA261
P	LYS115

---

site_id	SWS_FT_FI11
Number of Residues	4
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122

Chain	Residue	Details
O	GLY131
O	ASP192
P	GLY131
P	ASP192

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842

Chain	Residue	Details
O	TYR137
P	TYR137

---

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

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

Chain	Residue	Details
P	CYS149
P	HIS176

---