Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1CER

DETERMINANTS OF ENZYME THERMOSTABILITY OBSERVED IN THE MOLECULAR STRUCTURE OF THERMUS AQUATICUS D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE AT 2.5 ANGSTROMS RESOLUTION

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	0050661	molecular_function	NADP binding
A	0051287	molecular_function	NAD binding
B	0000166	molecular_function	nucleotide binding
B	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
B	0005737	cellular_component	cytoplasm
B	0006006	biological_process	glucose metabolic process
B	0006096	biological_process	glycolytic process
B	0016491	molecular_function	oxidoreductase activity
B	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B	0050661	molecular_function	NADP binding
B	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	0050661	molecular_function	NADP binding
C	0051287	molecular_function	NAD binding
D	0000166	molecular_function	nucleotide binding
D	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
D	0005737	cellular_component	cytoplasm
D	0006006	biological_process	glucose metabolic process
D	0006096	biological_process	glycolytic process
D	0016491	molecular_function	oxidoreductase activity
D	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D	0050661	molecular_function	NADP binding
D	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	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	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	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	0050661	molecular_function	NADP binding
R	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE NAD O 336

Chain	Residue
O	ASN6
O	THR96
O	GLY97
O	THR119
O	ALA120
O	CYS149
O	ASN313
O	TYR317
O	PHE8
O	GLY9
O	ARG10
O	ILE11
O	ASP32
O	LEU33
O	LYS77
O	SER95

site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE NAD P 336

Chain	Residue
P	ASN6
P	GLY7
P	GLY9
P	ARG10
P	ILE11
P	ASN31
P	ASP32
P	LEU33
P	SER95
P	THR96
P	GLY97
P	THR119
P	ALA120
P	CYS149
P	ASN180
P	ASN313
P	TYR317
Q	LEU187

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NAD Q 336

Chain	Residue
Q	ASN6
Q	GLY7
Q	GLY9
Q	ARG10
Q	ILE11
Q	ASN31
Q	ASP32
Q	LEU33
Q	LYS77
Q	SER95
Q	GLY97
Q	PHE99
Q	THR119
Q	ALA120
Q	CYS149
Q	THR179
Q	ASN180
Q	ASN313
Q	TYR317

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE NAD R 336

Chain	Residue
O	LEU187
R	ASN6
R	GLY7
R	GLY9
R	ARG10
R	ILE11
R	ASP32
R	LEU33
R	SER95
R	THR96
R	GLY97
R	THR119
R	ALA120
R	ASN180
R	ASN313
R	TYR317

site_id	AC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE NAD A 336

Chain	Residue
A	ASN6
A	PHE8
A	GLY9
A	ARG10
A	ILE11
A	ASP32
A	LEU33
A	LYS77
A	SER95
A	THR96
A	GLY97
A	THR119
A	ALA120
A	CYS149
A	ASN313
A	TYR317

site_id	AC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE NAD B 336

Chain	Residue
B	ASN180
B	ASN313
B	TYR317
C	LEU187
B	ASN6
B	GLY7
B	GLY9
B	ARG10
B	ILE11
B	ASN31
B	ASP32
B	LEU33
B	SER95
B	THR96
B	GLY97
B	THR119
B	ALA120
B	CYS149

site_id	AC7
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NAD C 336

Chain	Residue
C	ASN6
C	GLY7
C	GLY9
C	ARG10
C	ILE11
C	ASN31
C	ASP32
C	LEU33
C	LYS77
C	SER95
C	GLY97
C	PHE99
C	THR119
C	ALA120
C	CYS149
C	THR179
C	ASN180
C	ASN313
C	TYR317

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE NAD D 336

Chain	Residue
A	LEU187
D	ASN6
D	GLY7
D	GLY9
D	ARG10
D	ILE11
D	ASP32
D	LEU33
D	SER95
D	THR96
D	GLY97
D	THR119
D	ALA120
D	ASN180
D	ASN313
D	TYR317

Functional Information from PROSITE/UniProt

site_id	PS00071
Number of Residues	8
Details	GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNsL

Chain	Residue	Details
O	ALA147-LEU154

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"8611563","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8611563","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2006","submissionDatabase":"PDB data bank","title":"High resolution structures of Thermus aquaticus glyceraldehyde-3-phosphate dehydrogenase: role of 220's loop motion in catalysis.","authors":["Jenkins J.L.","Buencamino R.","Tanner J.J."]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2006","submissionDatabase":"PDB data bank","title":"High resolution structures of Thermus aquaticus glyceraldehyde-3-phosphate dehydrogenase: role of 220's loop motion in catalysis.","authors":["Jenkins J.L.","Buencamino R.","Tanner J.J."]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	48
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00362","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Site: {"description":"Activates thiol group during catalysis","evidences":[{"source":"PubMed","id":"8611563","evidenceCode":"ECO:0000305"}]}

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

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1szj

Chain	Residue	Details
A	CYS149
A	HIS176

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1szj

Chain	Residue	Details
B	CYS149
B	HIS176

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1szj

Chain	Residue	Details
C	CYS149
C	HIS176

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1szj

Chain	Residue	Details
D	CYS149
D	HIS176

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)