Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7C5Q

Crystal Structure of H177A mutant Glyceraldehyde-3-phosphate dehydrogenase1 from Escherichia coli complexed with BPG at 2.13 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	32
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	ASN315
O	PHE319
O	G3H402
O	GLY8
O	HOH510
O	HOH519
O	HOH551
O	HOH554
O	HOH566
O	HOH569
O	HOH631
O	HOH641
O	HOH645
O	HOH650
O	PHE9
O	HOH653
O	HOH673
O	HOH690
O	GLY10
O	ARG11
O	ILE12
O	ASN33
O	ASP34
O	LEU35

site_id	AC2
Number of Residues	9
Details	binding site for residue G3H O 402

Chain	Residue
O	THR180
O	THR182
O	HIS207
O	ARG232
O	NAD401
O	HOH510
O	HOH619
O	HOH687
O	HOH710

site_id	AC3
Number of Residues	6
Details	binding site for residue PO4 O 403

Chain	Residue
O	HIS163
O	GLY167
O	ILE168
O	GLU169
O	LEU222
O	LYS225

site_id	AC4
Number of Residues	3
Details	binding site for residue PO4 O 404

Chain	Residue
O	ASP274
O	GLU275
O	HOH512

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

Chain	Residue
O	ARG19
O	HIS286
O	ARG325
O	HOH557
O	HOH575

site_id	AC6
Number of Residues	2
Details	binding site for residue CL O 406

Chain	Residue
O	LYS227
O	GLY228

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

Chain	Residue
O	ALA80
O	LYS81
O	ALA108

site_id	AC8
Number of Residues	7
Details	binding site for residue PO4 O 408

Chain	Residue
O	ALA201
O	HOH580
P	ALA201
Q	ALA201
Q	HOH536
R	ALA201
R	HOH570

site_id	AC9
Number of Residues	34
Details	binding site for residue NAD P 401

Chain	Residue
P	HOH670
P	HOH678
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	DG4402
P	HOH502
P	HOH511
P	HOH530
P	HOH546
P	HOH553
P	HOH555
P	HOH606
P	HOH607
P	HOH612
P	HOH628
P	HOH629
P	HOH665

site_id	AD1
Number of Residues	15
Details	binding site for residue DG4 P 402

Chain	Residue
P	PRO122
P	THR180
P	THR182
P	HIS207
P	THR208
P	THR209
P	GLY210
P	ARG232
P	NAD401
P	HOH551
P	HOH553
P	HOH588
P	HOH665
P	HOH670
P	HOH689

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	3
Details	binding site for residue PO4 P 404

Chain	Residue
P	ASP274
P	GLU275
P	HOH643

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

Chain	Residue
O	HOH521
P	LYS227
P	GLY228
P	HOH713

site_id	AD5
Number of Residues	33
Details	binding site for residue NAD Q 401

Chain	Residue
Q	ASN7
Q	GLY8
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	ASN315
Q	PHE319
Q	G3H402
Q	HOH503
Q	HOH527
Q	HOH529
Q	HOH553
Q	HOH563
Q	HOH574
Q	HOH582
Q	HOH589
Q	HOH603
Q	HOH628
Q	HOH648
Q	HOH665
Q	HOH675
Q	HOH681

site_id	AD6
Number of Residues	8
Details	binding site for residue G3H Q 402

Chain	Residue
Q	THR180
Q	GLY181
Q	THR182
Q	ARG232
Q	NAD401
Q	HOH502
Q	HOH575
Q	HOH687

site_id	AD7
Number of Residues	4
Details	binding site for residue PO4 Q 403

Chain	Residue
Q	HIS163
Q	GLY167
Q	ILE168
Q	LYS225

site_id	AD8
Number of Residues	3
Details	binding site for residue PO4 Q 404

Chain	Residue
Q	ASP274
Q	GLU275
Q	HOH580

site_id	AD9
Number of Residues	4
Details	binding site for residue EDO Q 405

Chain	Residue
Q	ARG19
Q	HIS286
Q	ARG325
Q	HOH518

site_id	AE1
Number of Residues	4
Details	binding site for residue CL Q 406

Chain	Residue
Q	LYS227
Q	GLY228
Q	HOH674
R	HOH548

site_id	AE2
Number of Residues	31
Details	binding site for residue NAD R 401

Chain	Residue
R	ASN7
R	GLY8
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	CYS150
R	ASN315
R	PHE319
R	G3H402
R	HOH502
R	HOH507
R	HOH514
R	HOH538
R	HOH546
R	HOH568
R	HOH572
R	HOH575
R	HOH578
R	HOH588
R	HOH595
R	HOH608

site_id	AE3
Number of Residues	6
Details	binding site for residue G3H R 402

Chain	Residue
R	THR180
R	THR182
R	ARG232
R	NAD401
R	HOH502
R	HOH514

site_id	AE4
Number of Residues	6
Details	binding site for residue PO4 R 403

Chain	Residue
R	HIS163
R	GLY167
R	ILE168
R	GLU221
R	LEU222
R	LYS225

site_id	AE5
Number of Residues	3
Details	binding site for residue PO4 R 404

Chain	Residue
R	ASP274
R	GLU275
R	HOH509

site_id	AE6
Number of Residues	4
Details	binding site for residue EDO R 405

Chain	Residue
R	ARG19
R	HIS286
R	ARG325
R	HOH519

site_id	AE7
Number of Residues	3
Details	binding site for residue CL R 406

Chain	Residue
Q	HOH547
R	LYS227
R	GLY228

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)