3K9Q

Crystal structure of C151G mutant of Glyceraldehyde 3-phosphate dehydrogenase 1 from Methicillin resistant Staphylococcus aureus (MRSA252) at 2.5 angstrom resolution

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	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	24
Details	BINDING SITE FOR RESIDUE NAD Q 0

Chain	Residue
P	PRO190
Q	CYS96
Q	THR97
Q	GLY98
Q	SER120
Q	ALA121
Q	THR181
Q	ASN316
Q	TYR320
Q	GOL337
Q	HOH341
Q	GLY9
Q	HOH342
Q	HOH347
Q	HOH413
Q	HOH421
Q	HOH425
Q	GLY11
Q	ARG12
Q	ILE13
Q	ASN33
Q	ASP34
Q	LEU35
Q	PRO78

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL Q 337

Chain	Residue
Q	NAD0
Q	SER150
Q	GLY151
Q	THR152
Q	HIS178
Q	THR211
Q	HOH425

---

site_id	AC3
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAD O 0

Chain	Residue
O	GLY9
O	GLY11
O	ARG12
O	ILE13
O	ASN33
O	ASP34
O	PRO78
O	CYS96
O	THR97
O	GLY98
O	PHE99
O	SER120
O	ALA121
O	ASN316
O	TYR320
O	GOL337
O	CL338
O	HOH358
O	HOH366
O	HOH373
O	HOH381
O	HOH393
R	PRO190
R	HOH342

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL O 337

Chain	Residue
O	NAD0
O	ARG12
O	TYR180
O	THR181
O	GLY182
O	ALA238
O	THR239
O	ASN316
O	GLU317
R	GLN187

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL O 338

Chain	Residue
O	NAD0
O	THR181

---

site_id	AC6
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAD P 0

Chain	Residue
P	GLY9
P	GLY11
P	ARG12
P	ILE13
P	ASN33
P	ASP34
P	PRO78
P	CYS96
P	THR97
P	GLY98
P	PHE99
P	SER120
P	ALA121
P	THR181
P	ASN316
P	TYR320
P	GOL337
P	HOH338
P	HOH339
P	HOH370
P	HOH372
P	HOH395
P	HOH396
Q	PRO190

---

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL P 337

Chain	Residue
P	NAD0
P	SER150
P	GLY151
P	THR152
P	HIS178
P	TYR314
P	HOH394

---

site_id	AC8
Number of Residues	20
Details	BINDING SITE FOR RESIDUE NAD R 0

Chain	Residue
O	HOH430
R	GLY9
R	GLY11
R	ARG12
R	ILE13
R	ASN33
R	ASP34
R	PRO78
R	CYS96
R	THR97
R	GLY98
R	PHE99
R	SER120
R	ALA121
R	ASN316
R	TYR320
R	HOH356
R	HOH359
R	HOH378
O	PRO190

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
Q	MET300-TYR314

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"20620151","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20620151","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of Staphylococcal GAPDH1 in a hexagonal space group.","authors":["Roychowdhury A.","Mukherjee S.","Dutta D.","Das A.K."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20620151","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00362","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Site: {"description":"Activates thiol group during catalysis","evidences":[{"source":"PubMed","id":"20620151","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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