3KV3

Crystal structure of C151S mutant of Glyceraldehyde-3-phosphate dehydrogenase 1 (GAPDH 1)from methicillin resistant Staphylococcus aureus MRSA252 complexed with NAD and G3P

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	24
Details	BINDING SITE FOR RESIDUE NAD O 0

Chain	Residue
O	GLY9
O	THR97
O	GLY98
O	PHE99
O	SER120
O	ALA121
O	ASN316
O	TYR320
O	3PG337
O	HOH339
O	HOH351
O	GLY11
O	HOH357
O	HOH367
O	HOH385
R	PRO190
R	HOH343
O	ARG12
O	ILE13
O	ASN33
O	ASP34
O	LEU35
O	PRO78
O	CYS96

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 3PG O 337

Chain	Residue
O	NAD0
O	SER151
O	THR152
O	HIS178
O	THR181
O	ASP183
O	THR211
O	ARG234
O	HOH383

---

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

Chain	Residue
P	PRO190
P	HOH348
Q	GLY9
Q	GLY11
Q	ARG12
Q	ILE13
Q	ASN33
Q	ASP34
Q	LEU35
Q	PRO78
Q	CYS96
Q	THR97
Q	GLY98
Q	PHE99
Q	SER120
Q	ALA121
Q	ASN316
Q	TYR320
Q	3PG337
Q	HOH344
Q	HOH347
Q	HOH353
Q	HOH388
Q	HOH405

---

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 3PG Q 337

Chain	Residue
Q	NAD0
Q	SER151
Q	THR152
Q	HIS178
Q	THR181
Q	ASP183
Q	THR211
Q	ARG234
Q	HOH344
Q	HOH388
Q	HOH396

---

site_id	AC5
Number of Residues	20
Details	BINDING SITE FOR RESIDUE NAD R 0

Chain	Residue
O	PRO190
O	HOH338
R	GLY9
R	GLY11
R	ARG12
R	ILE13
R	ASN33
R	ASP34
R	LEU35
R	PRO78
R	CYS96
R	THR97
R	GLY98
R	PHE99
R	SER120
R	ALA121
R	ASN316
R	TYR320
R	3PG337
R	HOH387

---

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 3PG R 337

Chain	Residue
R	NAD0
R	SER150
R	SER151
R	THR152
R	HIS178
R	THR181
R	ASP183
R	ARG234
R	HOH394

---

site_id	AC7
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NAD P 0

Chain	Residue
P	ARG12
P	ILE13
P	ASN33
P	ASP34
P	LEU35
P	PRO78
P	CYS96
P	THR97
P	GLY98
P	PHE99
P	SER120
P	ALA121
P	ASN316
P	TYR320
P	3PG337
P	HOH351
Q	PRO190
P	GLY9
P	GLY11

---

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 3PG P 337

Chain	Residue
P	NAD0
P	SER151
P	THR152
P	HIS178
P	THR181
P	ASP183
P	THR211
P	ARG234

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
O	MET300-TYR314

---

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	SER151
Q	SER151
R	SER151
P	SER151

---

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
Q	ARG12
Q	ASP34
Q	SER120
R	ARG12
R	ASP34
R	SER120

---

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

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

---

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

Chain	Residue	Details
O	ARG198
Q	ARG198
R	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
Q	HIS178
R	HIS178
P	HIS178

---