Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7C5H

Crystal Structure of Glyceraldehyde-3-phosphate dehydrogenase1 from Escherichia coli at 2.09 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	7
Details	binding site for residue PO4 O 401

Chain	Residue
O	THR180
O	THR182
O	ARG232
O	NAD402
O	HOH532
O	HOH579
O	HOH629

site_id	AC2
Number of Residues	34
Details	binding site for residue NAD O 402

Chain	Residue
O	PHE9
O	GLY10
O	ARG11
O	ILE12
O	ASN33
O	ASP34
O	LEU35
O	LYS78
O	CYS96
O	THR97
O	GLY98
O	PHE99
O	SER120
O	ALA121
O	CYS150
O	ASN315
O	PHE319
O	PO4401
O	HOH505
O	HOH508
O	HOH532
O	HOH536
O	HOH545
O	HOH548
O	HOH578
O	HOH587
O	HOH604
O	HOH623
O	HOH638
O	HOH652
O	HOH661
O	HOH673
O	ASN7
O	GLY8

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	5
Details	binding site for residue CL O 404

Chain	Residue
O	HIS177
O	HIS207
O	ALA230
O	ARG232
O	HOH535

site_id	AC5
Number of Residues	5
Details	binding site for residue EDO O 405

Chain	Residue
O	ARG19
O	HIS286
O	ARG325
O	HOH613
O	HOH678

site_id	AC6
Number of Residues	3
Details	binding site for residue EDO O 406

Chain	Residue
O	ASP274
O	GLU275
O	HOH506

site_id	AC7
Number of Residues	3
Details	binding site for residue CL O 407

Chain	Residue
O	LYS227
O	GLY228
O	HOH619

site_id	AC8
Number of Residues	4
Details	binding site for residue CL O 408

Chain	Residue
O	ALA80
O	LYS81
O	ALA108
O	HOH581

site_id	AC9
Number of Residues	7
Details	binding site for residue PO4 P 401

Chain	Residue
P	THR180
P	THR182
P	ARG232
P	NAD402
P	HOH533
P	HOH615
P	HOH626

site_id	AD1
Number of Residues	34
Details	binding site for residue NAD P 402

Chain	Residue
P	HOH564
P	HOH585
P	HOH601
P	HOH626
P	HOH627
P	HOH636
P	HOH659
P	HOH664
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	CYS150
P	ASN315
P	PHE319
P	PO4401
P	HOH502
P	HOH507
P	HOH524
P	HOH533
P	HOH534
P	HOH537

site_id	AD2
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	AD3
Number of Residues	5
Details	binding site for residue PEG P 404

Chain	Residue
P	ASP164
P	SER165
P	PHE166
P	GLY167
P	LYS249

site_id	AD4
Number of Residues	4
Details	binding site for residue EDO P 405

Chain	Residue
P	ARG19
P	HIS286
P	ARG325
P	HOH573

site_id	AD5
Number of Residues	2
Details	binding site for residue EDO P 406

Chain	Residue
P	ASP274
P	GLU275

site_id	AD6
Number of Residues	3
Details	binding site for residue CL P 407

Chain	Residue
O	HOH540
P	LYS227
P	GLY228

site_id	AD7
Number of Residues	6
Details	binding site for residue PO4 Q 401

Chain	Residue
Q	THR180
Q	THR182
Q	ARG232
Q	NAD402
Q	HOH531
Q	HOH640

site_id	AD8
Number of Residues	33
Details	binding site for residue NAD Q 402

Chain	Residue
P	HOH558
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	CYS150
Q	ASN315
Q	PHE319
Q	PO4401
Q	HOH504
Q	HOH515
Q	HOH522
Q	HOH531
Q	HOH550
Q	HOH554
Q	HOH565
Q	HOH591
Q	HOH613
Q	HOH625
Q	HOH630
Q	HOH651
Q	HOH654

site_id	AD9
Number of Residues	5
Details	binding site for residue PO4 Q 403

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

site_id	AE1
Number of Residues	4
Details	binding site for residue GOL Q 404

Chain	Residue
Q	ARG19
Q	HIS286
Q	ARG325
Q	HOH502

site_id	AE2
Number of Residues	3
Details	binding site for residue EDO Q 405

Chain	Residue
Q	ASP274
Q	GLU275
Q	HOH512

site_id	AE3
Number of Residues	4
Details	binding site for residue CL Q 406

Chain	Residue
Q	LYS227
Q	GLY228
Q	HOH674
R	HOH519

site_id	AE4
Number of Residues	6
Details	binding site for residue PO4 R 401

Chain	Residue
R	THR180
R	THR182
R	ARG232
R	NAD402
R	PO4404
R	HOH512

site_id	AE5
Number of Residues	33
Details	binding site for residue NAD R 402

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	CYS150
R	ASN315
R	PHE319
R	PO4401
R	HOH510
R	HOH512
R	HOH513
R	HOH515
R	HOH529
R	HOH558
R	HOH566
R	HOH567
R	HOH569
R	HOH581
R	HOH590
R	HOH600

site_id	AE6
Number of Residues	5
Details	binding site for residue PO4 R 403

Chain	Residue
R	HIS163
R	GLY167
R	ILE168
R	GLU221
R	LYS225

site_id	AE7
Number of Residues	9
Details	binding site for residue PO4 R 404

Chain	Residue
R	SER149
R	CYS150
R	THR151
R	HIS177
R	THR209
R	ARG232
R	PO4401
R	HOH517
R	HOH595

site_id	AE8
Number of Residues	4
Details	binding site for residue EDO R 405

Chain	Residue
R	ARG19
R	HIS286
R	ARG325
R	HOH518

site_id	AE9
Number of Residues	3
Details	binding site for residue CL R 406

Chain	Residue
Q	HOH517
R	LYS227
R	GLY228

site_id	AF1
Number of Residues	3
Details	binding site for residue CL R 407

Chain	Residue
R	ALA80
R	LYS81
R	ALA108

Functional Information from PROSITE/UniProt

site_id	PS00071
Number of Residues	8
Details	GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL

Chain	Residue	Details
O	ALA148-LEU155

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)