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
O	0072524	biological_process	pyridine-containing compound metabolic process
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
P	0072524	biological_process	pyridine-containing compound metabolic process

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	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10978154","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10978154","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19542219","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8636984","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2004","submissionDatabase":"PDB data bank","title":"Crystal structure of MES buffer bound form of glyceraldehyde 3-phosphate dehydrogenase from Escherichia coli.","authors":["Shin D.H.","Thor J.","Yokota H.","Kim R.","Kim S.H."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10978154","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19542219","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8636984","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10978154","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19542219","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19542219","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10978154","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00362","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19542219","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2004","submissionDatabase":"PDB data bank","title":"Crystal structure of MES buffer bound form of glyceraldehyde 3-phosphate dehydrogenase from Escherichia coli.","authors":["Shin D.H.","Thor J.","Yokota H.","Kim R.","Kim S.H."]}},{"source":"PubMed","id":"10978154","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Site: {"description":"Activates thiol group during catalysis","evidences":[{"source":"PubMed","id":"2659073","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	16
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	6
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}

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

---