7C5K

Crystal Structure of C150S mutant of Glyceraldehyde-3-phosphate-dehydrogenase1 from Escherichia coli complexed with G3P at 2.69 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	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	0042802	molecular_function	identical protein 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	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	0042802	molecular_function	identical protein 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	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	0042802	molecular_function	identical protein 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	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	0042802	molecular_function	identical protein binding
R	0050661	molecular_function	NADP binding
R	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	28
Details	binding site for residue NAD O 401

Chain	Residue
O	ASN7
O	LYS78
O	CYS96
O	THR97
O	GLY98
O	PHE99
O	SER120
O	ALA121
O	SER150
O	THR180
O	ASN315
O	GLY8
O	PHE319
O	G3H402
O	HOH513
O	HOH533
O	HOH537
O	HOH543
O	HOH559
O	HOH588
O	HOH615
O	PHE9
O	GLY10
O	ARG11
O	ILE12
O	ASN33
O	ASP34
O	LEU35

---

site_id	AC2
Number of Residues	10
Details	binding site for residue G3H O 402

Chain	Residue
O	SER149
O	SER150
O	THR151
O	HIS177
O	THR180
O	THR182
O	THR209
O	ARG232
O	NAD401
O	HOH609

---

site_id	AC3
Number of Residues	5
Details	binding site for residue PO4 O 403

Chain	Residue
O	HIS163
O	GLY167
O	ILE168
O	GLU169
O	LYS225

---

site_id	AC4
Number of Residues	9
Details	binding site for residue PO4 O 404

Chain	Residue
O	ALA201
O	GLU202
O	HOH562
P	ALA201
P	HOH556
P	HOH567
P	HOH574
Q	ALA201
R	ALA201

---

site_id	AC5
Number of Residues	26
Details	binding site for residue NAD P 401

Chain	Residue
P	ASN7
P	GLY8
P	PHE9
P	GLY10
P	ARG11
P	ILE12
P	ASP34
P	LEU35
P	LYS78
P	CYS96
P	THR97
P	GLY98
P	SER120
P	ALA121
P	THR180
P	ASN315
P	PHE319
P	G3H402
P	HOH501
P	HOH502
P	HOH513
P	HOH520
P	HOH531
P	HOH534
P	HOH542
P	HOH546

---

site_id	AC6
Number of Residues	8
Details	binding site for residue G3H P 402

Chain	Residue
P	SER149
P	SER150
P	THR151
P	HIS177
P	THR180
P	THR182
P	ARG232
P	NAD401

---

site_id	AC7
Number of Residues	5
Details	binding site for residue PO4 P 403

Chain	Residue
P	HIS163
P	GLY167
P	ILE168
P	LEU222
P	LYS225

---

site_id	AC8
Number of Residues	30
Details	binding site for residue NAD Q 401

Chain	Residue
Q	LYS78
Q	CYS96
Q	THR97
Q	GLY98
Q	PHE99
Q	SER120
Q	ALA121
Q	SER150
Q	THR180
Q	ASN315
Q	PHE319
Q	3PG402
Q	HOH502
Q	HOH512
Q	HOH522
Q	HOH526
Q	HOH531
Q	HOH552
Q	HOH555
Q	HOH562
Q	HOH577
Q	HOH581
Q	ASN7
Q	GLY8
Q	PHE9
Q	GLY10
Q	ARG11
Q	ILE12
Q	ASP34
Q	LEU35

---

site_id	AC9
Number of Residues	11
Details	binding site for residue 3PG Q 402

Chain	Residue
Q	SER149
Q	SER150
Q	THR151
Q	HIS177
Q	THR180
Q	THR182
Q	THR209
Q	ARG232
Q	NAD401
Q	HOH512
Q	HOH553

---

site_id	AD1
Number of Residues	6
Details	binding site for residue PO4 Q 403

Chain	Residue
Q	HIS163
Q	GLY167
Q	ILE168
Q	GLU221
Q	LEU222
Q	LYS225

---

site_id	AD2
Number of Residues	26
Details	binding site for residue NAD R 401

Chain	Residue
R	ASN7
R	GLY8
R	PHE9
R	GLY10
R	ARG11
R	ILE12
R	ASN33
R	ASP34
R	LYS78
R	CYS96
R	THR97
R	GLY98
R	PHE99
R	SER120
R	ALA121
R	THR180
R	ASN315
R	PHE319
R	3PG402
R	HOH501
R	HOH503
R	HOH513
R	HOH525
R	HOH529
R	HOH553
R	HOH558

---

site_id	AD3
Number of Residues	11
Details	binding site for residue 3PG R 402

Chain	Residue
R	SER149
R	SER150
R	THR151
R	HIS177
R	THR180
R	THR182
R	THR209
R	ARG232
R	NAD401
R	HOH525
R	HOH545

---

site_id	AD4
Number of Residues	4
Details	binding site for residue PO4 R 403

Chain	Residue
R	HIS163
R	GLY167
R	ILE168
R	LYS225

---

Functional Information from PROSITE/UniProt

site_id	PS00430
Number of Residues	89
Details	TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. hhhhhhssglvprgshmasmskvgingfgrigrlvlrrllevksnidvvaindltspkilayllkhdsnygpfpwsvdfte..................................DSLIVDGK

Chain	Residue	Details
O	HIS-18-LYS70

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