7C5J

Crystal Structure of C150A mutant of Glyceraldehyde-3-phosphate dehydrogenase1 from Escherichia coli at 1.98 Angstrom resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
O	0006006	biological_process	glucose metabolic process
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	0006006	biological_process	glucose metabolic process
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	0006006	biological_process	glucose metabolic process
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	0006006	biological_process	glucose metabolic process
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	35
Details	binding site for residue NAD O 401

Chain	Residue
O	ASN7
O	GLU77
O	LYS78
O	CYS96
O	THR97
O	GLY98
O	PHE99
O	SER120
O	ALA121
O	ALA150
O	THR180
O	GLY8
O	ASN315
O	PHE319
O	HOH503
O	HOH513
O	HOH542
O	HOH557
O	HOH574
O	HOH578
O	HOH634
O	HOH635
O	PHE9
O	HOH639
O	HOH658
O	HOH679
O	HOH680
O	HOH685
O	HOH696
O	GLY10
O	ARG11
O	ILE12
O	ASN33
O	ASP34
O	LEU35

---

site_id	AC2
Number of Residues	4
Details	binding site for residue EDO O 402

Chain	Residue
O	GLU104
Q	PHE54
Q	PRO55
Q	TRP56

---

site_id	AC3
Number of Residues	33
Details	binding site for residue NAD P 401

Chain	Residue
P	ASN7
P	GLY8
P	PHE9
P	GLY10
P	ARG11
P	ILE12
P	ASN33
P	ASP34
P	LEU35
P	LYS78
P	CYS96
P	THR97
P	GLY98
P	PHE99
P	SER120
P	ALA121
P	ALA150
P	THR180
P	ASN315
P	PHE319
P	HOH507
P	HOH519
P	HOH529
P	HOH534
P	HOH562
P	HOH576
P	HOH613
P	HOH624
P	HOH636
P	HOH662
P	HOH666
P	HOH678
P	HOH689

---

site_id	AC4
Number of Residues	31
Details	binding site for residue NAD Q 401

Chain	Residue
Q	HOH666
Q	HOH675
Q	HOH688
Q	HOH689
Q	ASN7
Q	GLY8
Q	GLY10
Q	ARG11
Q	ILE12
Q	ASN33
Q	ASP34
Q	LYS78
Q	CYS96
Q	THR97
Q	GLY98
Q	PHE99
Q	SER120
Q	ALA121
Q	ALA150
Q	THR180
Q	ASN315
Q	PHE319
Q	HOH505
Q	HOH537
Q	HOH539
Q	HOH575
Q	HOH582
Q	HOH598
Q	HOH606
Q	HOH623
Q	HOH659

---

site_id	AC5
Number of Residues	4
Details	binding site for residue EDO Q 402

Chain	Residue
Q	SER25
Q	ASN26
Q	ILE27
Q	ASP28

---

site_id	AC6
Number of Residues	32
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	ALA150
R	THR180
R	ASN315
R	PHE319
R	HOH502
R	HOH507
R	HOH532
R	HOH534
R	HOH541
R	HOH550
R	HOH565
R	HOH567
R	HOH581
R	HOH609
R	HOH615
R	HOH619
R	HOH639

---

site_id	AC7
Number of Residues	4
Details	binding site for residue EDO R 402

Chain	Residue
R	ASP59
R	PHE60
R	HOH660
R	HOH703

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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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