3LC7

Crystal Structure of apo Glyceraldehyde-3-phosphate dehydrogenase 1 (GAPDH1) from methicllin resistant Staphylococcus aureus (MRSA252)

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 GOL O 337

Chain	Residue
O	GLY11
O	ARG12
O	ILE13
O	HOH343
R	HOH378

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL Q 337

Chain	Residue
Q	GLY11
Q	ARG12
Q	ILE13

---

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	ALA149-LEU156

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site_id	PS00211
Number of Residues	15
Details	ABC_TRANSPORTER_1 ABC transporters family signature. MSVGDRQLVKVAAWY

Chain	Residue	Details
O	MET300-TYR314

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:20620151

Chain	Residue	Details
O	CYS151
R	CYS151
Q	CYS151
P	CYS151

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:20620151, ECO:0000269|Ref.3

Chain	Residue	Details
O	ARG12
P	ARG12
P	ASP34
P	SER120
O	ASP34
O	SER120
R	ARG12
R	ASP34
R	SER120
Q	ARG12
Q	ASP34
Q	SER120

---

site_id	SWS_FT_FI3
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269|PubMed:20620151

Chain	Residue	Details
O	SER150
R	ASN316
Q	SER150
Q	THR181
Q	THR211
Q	ARG234
Q	ASN316
P	SER150
P	THR181
P	THR211
P	ARG234
O	THR181
P	ASN316
O	THR211
O	ARG234
O	ASN316
R	SER150
R	THR181
R	THR211
R	ARG234

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P00362

Chain	Residue	Details
O	ARG198
R	ARG198
Q	ARG198
P	ARG198

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	SITE: Activates thiol group during catalysis => ECO:0000269|PubMed:20620151

Chain	Residue	Details
O	HIS178
R	HIS178
Q	HIS178
P	HIS178

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