7C5M

Crystal Structure of C150A+H177A mutant of Glyceraldehyde-3-phosphate-dehydrogenase1 from Escherichia coli complexed with G3P at 1.8 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	36
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	ALA150
O	ASN315
O	PHE319
O	GLY8
O	3PG402
O	HOH503
O	HOH521
O	HOH529
O	HOH533
O	HOH551
O	HOH585
O	HOH593
O	HOH631
O	HOH638
O	PHE9
O	HOH641
O	HOH670
O	HOH704
O	HOH709
O	HOH725
O	HOH736
O	HOH768
O	GLY10
O	ARG11
O	ILE12
O	ASN33
O	ASP34
O	LEU35

---

site_id	AC2
Number of Residues	13
Details	binding site for residue 3PG O 402

Chain	Residue
O	THR180
O	THR182
O	HIS207
O	THR208
O	ARG232
O	NAD401
O	HOH515
O	HOH577
O	HOH585
O	HOH604
O	HOH641
O	HOH721
O	HOH768

---

site_id	AC3
Number of Residues	7
Details	binding site for residue PO4 O 403

Chain	Residue
O	HIS163
O	GLY167
O	ILE168
O	GLU169
O	LYS225
O	HOH680
O	HOH749

---

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

Chain	Residue
O	ALA201
O	HOH633
P	ALA201
Q	ALA201
Q	HOH610
R	ALA201
R	HOH601

---

site_id	AC5
Number of Residues	36
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	ASN315
P	PHE319
P	G3H402
P	HOH510
P	HOH523
P	HOH530
P	HOH534
P	HOH556
P	HOH564
P	HOH587
P	HOH596
P	HOH600
P	HOH610
P	HOH648
P	HOH653
P	HOH669
P	HOH691
P	HOH740
P	HOH742

---

site_id	AC6
Number of Residues	10
Details	binding site for residue G3H P 402

Chain	Residue
P	THR180
P	THR182
P	HIS207
P	ARG232
P	NAD401
P	HOH523
P	HOH556
P	HOH742
P	HOH751
P	HOH756

---

site_id	AC7
Number of Residues	6
Details	binding site for residue EDO P 403

Chain	Residue
P	ARG19
P	HIS286
P	ARG325
P	HOH506
P	HOH768
P	HOH805

---

site_id	AC8
Number of Residues	35
Details	binding site for residue NAD Q 401

Chain	Residue
Q	ASN7
Q	GLY8
Q	PHE9
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	ASN315
Q	PHE319
Q	G3H402
Q	HOH503
Q	HOH515
Q	HOH530
Q	HOH557
Q	HOH559
Q	HOH569
Q	HOH572
Q	HOH585
Q	HOH597
Q	HOH602
Q	HOH615
Q	HOH635
Q	HOH689
Q	HOH734
Q	HOH736
Q	HOH758

---

site_id	AC9
Number of Residues	15
Details	binding site for residue G3H Q 402

Chain	Residue
Q	SER149
Q	ALA150
Q	THR151
Q	THR180
Q	THR182
Q	ARG232
Q	NAD401
Q	HOH501
Q	HOH554
Q	HOH557
Q	HOH559
Q	HOH635
Q	HOH659
Q	HOH688
Q	HOH763

---

site_id	AD1
Number of Residues	3
Details	binding site for residue EDO Q 403

Chain	Residue
Q	ASP274
Q	GLU275
Q	HOH573

---

site_id	AD2
Number of Residues	5
Details	binding site for residue EDO Q 404

Chain	Residue
Q	ARG19
Q	HIS286
Q	ARG325
Q	HOH502
Q	HOH636

---

site_id	AD3
Number of Residues	36
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	GLU77
R	LYS78
R	CYS96
R	THR97
R	GLY98
R	PHE99
R	SER120
R	ALA121
R	ALA150
R	ASN315
R	PHE319
R	G3H402
R	HOH505
R	HOH511
R	HOH515
R	HOH560
R	HOH561
R	HOH565
R	HOH582
R	HOH592
R	HOH594
R	HOH604
R	HOH607
R	HOH613
R	HOH623
R	HOH665
R	HOH690

---

site_id	AD4
Number of Residues	12
Details	binding site for residue G3H R 402

Chain	Residue
R	THR180
R	THR182
R	HIS207
R	ARG232
R	NAD401
R	HOH511
R	HOH514
R	HOH607
R	HOH608
R	HOH674
R	HOH690
R	HOH704

---

site_id	AD5
Number of Residues	4
Details	binding site for residue EDO R 403

Chain	Residue
R	ARG19
R	HIS286
R	ARG325
R	HOH519

---

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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