Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2GD1

COENZYME-INDUCED CONFORMATIONAL CHANGES IN GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM BACILLUS STEAROTHERMOPHILLUS

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	ABO
Number of Residues	3
Details	RESIDUES INTERACT WITH THE ADENINE BASE OF NAD

Chain	Residue
O	LEU33
O	THR96
O	ARG77

site_id	ABP
Number of Residues	3
Details	RESIDUES INTERACT WITH THE ADENINE BASE OF NAD

Chain	Residue
P	LEU33
P	THR96
P	ARG77

site_id	ABQ
Number of Residues	3
Details	RESIDUES INTERACT WITH THE ADENINE BASE OF NAD

Chain	Residue
Q	LEU33
Q	THR96
Q	ARG77

site_id	ABR
Number of Residues	3
Details	RESIDUES INTERACT WITH THE ADENINE BASE OF NAD

Chain	Residue
R	LEU33
R	THR96
R	ARG77

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 O 338

Chain	Residue
O	THR179
O	ASP181
O	ARG195
O	ARG231
O	HOH433

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 O 339

Chain	Residue
O	SER148
O	THR150
O	THR208
O	GLY209
O	ALA210
O	HOH376
O	HOH410

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 P 338

Chain	Residue
P	THR179
P	ASP181
P	ARG195
P	ARG231

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 P 339

Chain	Residue
P	SER148
P	THR208
P	GLY209
P	ALA210
P	HOH383
P	HOH440

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 Q 338

Chain	Residue
Q	THR179
Q	ASP181
Q	ARG195
Q	ARG231
Q	HOH412

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	HOH390

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 R 338

Chain	Residue
R	THR179
R	ASN180
R	ASP181
R	ARG195
R	ARG231

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 R 339

Chain	Residue
R	GLY209
R	ALA210
R	HOH393
R	HOH399
R	HOH460
R	SER148
R	THR208

site_id	APO
Number of Residues	2
Details	RESIDUES INTERACT WITH PHOSPHATE OF THE ADENOSINE NUCLEOTIDE OF NAD

Chain	Residue
O	ARG10
O	ASN180

site_id	APP
Number of Residues	2
Details	RESIDUES INTERACT WITH PHOSPHATE OF THE ADENOSINE NUCLEOTIDE OF NAD

Chain	Residue
P	ARG10
P	ASN180

site_id	APQ
Number of Residues	2
Details	RESIDUES INTERACT WITH PHOSPHATE OF THE ADENOSINE NUCLEOTIDE OF NAD

Chain	Residue
Q	ARG10
Q	ASN180

site_id	APR
Number of Residues	2
Details	RESIDUES INTERACT WITH PHOSPHATE OF THE ADENOSINE NUCLEOTIDE OF NAD

Chain	Residue
R	ARG10
R	ASN180

site_id	ARO
Number of Residues	1
Details	RESIDUES INTERACT WITH THE ADENOSINE RIBOSE OF NAD

Chain	Residue
O	ASP32

site_id	ARP
Number of Residues	1
Details	RESIDUES INTERACT WITH THE ADENOSINE RIBOSE OF NAD

Chain	Residue
P	ASP32

site_id	ARQ
Number of Residues	1
Details	RESIDUES INTERACT WITH THE ADENOSINE RIBOSE OF NAD

Chain	Residue
Q	ASP32

site_id	ARR
Number of Residues	1
Details	RESIDUES INTERACT WITH THE ADENOSINE RIBOSE OF NAD

Chain	Residue
R	ASP32

site_id	CTO
Number of Residues	2
Details	RESIDUES INVOLVED IN CATALYSIS

Chain	Residue
O	CYS149
O	HIS176

site_id	CTP
Number of Residues	2
Details	RESIDUES INVOLVED IN CATALYSIS

Chain	Residue
P	CYS149
P	HIS176

site_id	CTQ
Number of Residues	2
Details	RESIDUES INVOLVED IN CATALYSIS

Chain	Residue
Q	CYS149
Q	HIS176

site_id	CTR
Number of Residues	2
Details	RESIDUES INVOLVED IN CATALYSIS

Chain	Residue
R	CYS149
R	HIS176

site_id	NBO
Number of Residues	5
Details	RESIDUES INTERACT WITH THE NICOTINAMIDE BASE OF NAD

Chain	Residue
O	ILE11
O	CYS149
O	SER119
O	ASN313
O	TYR317

site_id	NBP
Number of Residues	5
Details	RESIDUES INTERACT WITH THE NICOTINAMIDE BASE OF NAD

Chain	Residue
P	ILE11
P	CYS149
P	SER119
P	ASN313
P	TYR317

site_id	NBQ
Number of Residues	5
Details	RESIDUES INTERACT WITH THE NICOTINAMIDE BASE OF NAD

Chain	Residue
Q	ILE11
Q	CYS149
Q	SER119
Q	ASN313
Q	TYR317

site_id	NBR
Number of Residues	5
Details	RESIDUES INTERACT WITH THE NICOTINAMIDE BASE OF NAD

Chain	Residue
R	ILE11
R	CYS149
R	SER119
R	ASN313
R	TYR317

site_id	NPO
Number of Residues	1
Details	RESIDUES INTERACT WITH THE PHOSPHATE OF THE NICOTINAMIDE NUCLEOTIDE OF NAD

Chain	Residue
O	ILE11

site_id	NPP
Number of Residues	1
Details	RESIDUES INTERACT WITH THE PHOSPHATE OF THE NICOTINAMIDE NUCLEOTIDE OF NAD

Chain	Residue
P	ILE11

site_id	NPQ
Number of Residues	1
Details	RESIDUES INTERACT WITH THE PHOSPHATE OF THE NICOTINAMIDE NUCLEOTIDE OF NAD

Chain	Residue
Q	ILE11

site_id	NPR
Number of Residues	1
Details	RESIDUES INTERACT WITH THE PHOSPHATE OF THE NICOTINAMIDE NUCLEOTIDE OF NAD

Chain	Residue
R	ILE11

site_id	NRO
Number of Residues	1
Details	RESIDUES INTERACT WITH THE RIBOSE OF THE NICOTINAMIDE NUCLEOTIDE OF NAD

Chain	Residue
O	SER119

site_id	NRP
Number of Residues	1
Details	RESIDUES INTERACT WITH THE RIBOSE OF THE NICOTINAMIDE NUCLEOTIDE OF NAD

Chain	Residue
P	SER119

site_id	NRQ
Number of Residues	1
Details	RESIDUES INTERACT WITH THE RIBOSE OF THE NICOTINAMIDE NUCLEOTIDE OF NAD

Chain	Residue
Q	SER119

site_id	NRR
Number of Residues	1
Details	RESIDUES INTERACT WITH THE RIBOSE OF THE NICOTINAMIDE NUCLEOTIDE OF NAD

Chain	Residue
R	SER119

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)