7C5L

Crystal Structure of C150S mutant of Glyceraldehyde-3-phosphate-dehydrogenase1 from Escherichia coli at 2.1 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	LYS78
O	CYS96
O	THR97
O	GLY98
O	PHE99
O	SER120
O	ALA121
O	SER150
O	THR180
O	ASN315
O	GLY8
O	PHE319
O	HOH506
O	HOH513
O	HOH516
O	HOH528
O	HOH535
O	HOH559
O	HOH595
O	HOH616
O	HOH629
O	PHE9
O	HOH645
O	HOH657
O	HOH659
O	HOH662
O	HOH676
O	HOH706
O	GLY10
O	ARG11
O	ILE12
O	ASN33
O	ASP34
O	LEU35

---

site_id	AC2
Number of Residues	3
Details	binding site for residue CL O 402

Chain	Residue
O	ALA80
O	LYS81
O	ALA108

---

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

Chain	Residue
O	HIS177
O	HIS207
O	ALA230
O	ARG232
O	HOH614

---

site_id	AC4
Number of Residues	7
Details	binding site for residue PO4 O 404

Chain	Residue
O	ALA201
O	HOH546
O	HOH589
P	ALA201
P	HOH654
Q	ALA201
R	ALA201

---

site_id	AC5
Number of Residues	34
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	SER150
P	THR180
P	ASN315
P	PHE319
P	HOH509
P	HOH517
P	HOH520
P	HOH526
P	HOH531
P	HOH576
P	HOH607
P	HOH627
P	HOH655
P	HOH661
P	HOH662
P	HOH673
P	HOH704
P	HOH705

---

site_id	AC6
Number of Residues	5
Details	binding site for residue CL P 402

Chain	Residue
P	HIS177
P	HIS207
P	ALA230
P	ARG232
P	HOH643

---

site_id	AC7
Number of Residues	3
Details	binding site for residue EDO P 403

Chain	Residue
P	ARG18
P	GLU22
P	HOH641

---

site_id	AC8
Number of Residues	33
Details	binding site for residue NAD Q 401

Chain	Residue
Q	ASP34
Q	LEU35
Q	LYS78
Q	CYS96
Q	THR97
Q	GLY98
Q	PHE99
Q	SER120
Q	ALA121
Q	SER150
Q	THR180
Q	ASN315
Q	PHE319
Q	HOH514
Q	HOH519
Q	HOH521
Q	HOH527
Q	HOH538
Q	HOH600
Q	HOH605
Q	HOH615
Q	HOH621
Q	HOH644
Q	HOH655
Q	HOH668
Q	HOH684
P	HOH561
Q	ASN7
Q	GLY8
Q	GLY10
Q	ARG11
Q	ILE12
Q	ASN33

---

site_id	AC9
Number of Residues	5
Details	binding site for residue CL Q 402

Chain	Residue
Q	HIS177
Q	HIS207
Q	ALA230
Q	ARG232
Q	HOH534

---

site_id	AD1
Number of Residues	33
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	LEU35
R	LYS78
R	CYS96
R	THR97
R	GLY98
R	PHE99
R	SER120
R	ALA121
R	SER150
R	ASN315
R	PHE319
R	HOH502
R	HOH511
R	HOH514
R	HOH542
R	HOH550
R	HOH554
R	HOH573
R	HOH578
R	HOH580
R	HOH585
R	HOH593
R	HOH607
R	HOH619
R	HOH625

---

site_id	AD2
Number of Residues	5
Details	binding site for residue CL R 402

Chain	Residue
R	HIS177
R	HIS207
R	ALA230
R	ARG232
R	HOH557

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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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