Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7C7K

Crystal Structure of Thioacyl-Glyceraldehyde-3-phosphate dehydrogenase 1(GAPDH 1) from Escherichia coli at 1.77 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	11
Details	binding site for residue G3H O 401

Chain	Residue
O	SER149
O	HOH599
O	HOH704
O	CYS150
O	THR151
O	HIS177
O	THR180
O	THR209
O	PEG407
O	HOH524
O	HOH531

site_id	AC2
Number of Residues	5
Details	binding site for residue PO4 O 402

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

site_id	AC3
Number of Residues	3
Details	binding site for residue EDO O 403

Chain	Residue
O	ASP274
O	GLU275
O	HOH723

site_id	AC4
Number of Residues	5
Details	binding site for residue EDO O 404

Chain	Residue
O	ARG19
O	HIS286
O	ARG325
O	HOH652
O	HOH737

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

Chain	Residue
O	GLU77
O	LYS78
O	GLU79
O	ASN82
O	HOH566

site_id	AC6
Number of Residues	8
Details	binding site for residue PO4 O 406

Chain	Residue
O	ALA201
O	HOH534
O	HOH598
P	ALA201
Q	ALA201
R	ALA201
R	HOH591
R	HOH653

site_id	AC7
Number of Residues	10
Details	binding site for residue PEG O 407

Chain	Residue
O	PRO122
O	SER149
O	THR152
O	THR209
O	GLY210
O	ALA211
O	G3H401
O	HOH508
O	HOH512
O	HOH736

site_id	AC8
Number of Residues	3
Details	binding site for residue EDO P 402

Chain	Residue
P	SER165
P	PHE166
P	LYS249

site_id	AC9
Number of Residues	4
Details	binding site for residue EDO P 403

Chain	Residue
P	ASN315
P	GLU316
P	G3H401
P	HOH505

site_id	AD1
Number of Residues	5
Details	binding site for residue ACN P 404

Chain	Residue
P	THR180
P	THR182
P	ARG232
P	G3H401
P	HOH765

site_id	AD2
Number of Residues	6
Details	binding site for residue EDO P 405

Chain	Residue
P	ARG19
P	HIS286
P	ARG325
P	HOH513
P	HOH623
P	HOH702

site_id	AD3
Number of Residues	33
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	LEU35
Q	LYS78
Q	CYS96
Q	THR97
Q	GLY98
Q	PHE99
Q	SER120
Q	ALA121
Q	CYS150
Q	THR180
Q	ASN315
Q	PHE319
Q	G3H402
Q	ACN406
Q	HOH502
Q	HOH503
Q	HOH528
Q	HOH550
Q	HOH552
Q	HOH566
Q	HOH610
Q	HOH644
Q	HOH648
Q	HOH672
Q	HOH683

site_id	AD4
Number of Residues	7
Details	binding site for residue EDO Q 403

Chain	Residue
Q	GLU268
Q	HIS286
Q	ARG325
Q	HOH567
Q	HOH690
Q	HOH702
Q	ARG19

site_id	AD5
Number of Residues	7
Details	binding site for residue EDO Q 404

Chain	Residue
Q	ILE246
Q	LEU247
Q	ASP303
Q	LEU304
Q	GLN305
Q	HOH591
Q	HOH682

site_id	AD6
Number of Residues	3
Details	binding site for residue EDO Q 405

Chain	Residue
Q	ASP274
Q	GLU275
Q	HOH592

site_id	AD7
Number of Residues	6
Details	binding site for residue ACN Q 406

Chain	Residue
Q	THR180
Q	THR182
Q	ARG232
Q	NAD401
Q	G3H402
Q	HOH566

site_id	AD8
Number of Residues	7
Details	binding site for residue EDO Q 407

Chain	Residue
Q	THR264
Q	ASN267
Q	PHE270
Q	GLY271
Q	TYR272
Q	PHE287
Q	HOH620

site_id	AD9
Number of Residues	8
Details	binding site for residue NAD R 402

Chain	Residue
R	GLY10
R	ARG11
R	ILE12
R	CYS96
R	HOH626
R	HOH629
R	HOH654
R	HOH656

site_id	AE1
Number of Residues	7
Details	binding site for residue EDO R 403

Chain	Residue
R	ARG19
R	GLU268
R	HIS286
R	ARG325
R	HOH548
R	HOH612
R	HOH664

site_id	AE2
Number of Residues	2
Details	binding site for residue PEG R 404

Chain	Residue
R	GLN107
R	ILE144

site_id	AE3
Number of Residues	4
Details	binding site for residue EDO R 405

Chain	Residue
R	ASP274
R	GLU275
R	HOH583
R	HOH604

site_id	AE4
Number of Residues	5
Details	binding site for residue ACN R 406

Chain	Residue
R	THR180
R	THR182
R	ARG232
R	G3H401
R	HOH741

site_id	AE5
Number of Residues	19
Details	binding site for Di-peptide G3H P 401 and CYS P 150

Chain	Residue
P	SER149
P	THR151
P	THR152
P	ASN153
P	CYS154
P	HIS177
P	THR180
P	THR209
P	GLY210
P	TYR313
P	ASN315
P	PHE319
P	EDO403
P	ACN404
P	HOH519
P	HOH600
P	HOH611
P	HOH639
P	HOH649

site_id	AE6
Number of Residues	18
Details	binding site for Di-peptide G3H Q 402 and CYS Q 150

Chain	Residue
Q	SER149
Q	THR151
Q	THR152
Q	ASN153
Q	CYS154
Q	HIS177
Q	THR180
Q	THR209
Q	GLY210
Q	TYR313
Q	ASN315
Q	PHE319
Q	NAD401
Q	ACN406
Q	HOH505
Q	HOH534
Q	HOH541
Q	HOH663

site_id	AE7
Number of Residues	19
Details	binding site for Di-peptide G3H R 401 and CYS R 150

Chain	Residue
R	SER149
R	THR151
R	THR152
R	ASN153
R	CYS154
R	HIS177
R	THR180
R	THR209
R	GLY210
R	TYR313
R	ASN315
R	PHE319
R	ACN406
R	HOH515
R	HOH544
R	HOH562
R	HOH566
R	HOH570
R	HOH643

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)