Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6M5X

A fungal glyceraldehyde-3-phosphate dehydrogenase with self-resistance to inhibitor heptelidic acid

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	0005829	cellular_component	cytosol
O	0006006	biological_process	glucose metabolic process
O	0006096	biological_process	glycolytic 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	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	0005829	cellular_component	cytosol
P	0006006	biological_process	glucose metabolic process
P	0006096	biological_process	glycolytic 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	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	0005829	cellular_component	cytosol
Q	0006006	biological_process	glucose metabolic process
Q	0006096	biological_process	glycolytic 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	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	0005829	cellular_component	cytosol
R	0006006	biological_process	glucose metabolic process
R	0006096	biological_process	glycolytic 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	0050661	molecular_function	NADP binding
R	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue EDO O 401

Chain	Residue
O	TYR253
O	ILE299
O	ALA300

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

Chain	Residue
O	ASP278
O	LYS296
P	TRP194

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

Chain	Residue
O	MET229
P	ASP278
P	LYS296
O	ARG195
O	SER207
O	SER208

site_id	AC4
Number of Residues	4
Details	binding site for residue EDO O 404

Chain	Residue
O	ARG321
O	ASP324
O	HOH519
O	HOH524

site_id	AC5
Number of Residues	4
Details	binding site for residue EDO O 405

Chain	Residue
O	ALA125
O	ALA127
Q	PRO220
Q	GOL406

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

Chain	Residue
O	TYR48
Q	HOH554

site_id	AC7
Number of Residues	2
Details	binding site for residue EDO O 407

Chain	Residue
O	THR209
O	GLY210

site_id	AC8
Number of Residues	6
Details	binding site for residue GOL O 408

Chain	Residue
O	GLY133
O	VAL134
O	ASN135
O	GLU136
O	ASP137
O	HOH558

site_id	AC9
Number of Residues	33
Details	binding site for residue NAD O 409

Chain	Residue
O	ASN8
O	GLY9
O	PHE10
O	GLY11
O	ARG12
O	ILE13
O	ASN33
O	ASP34
O	PRO35
O	PHE36
O	ARG79
O	SER97
O	THR98
O	GLY99
O	PHE101
O	SER121
O	ALA122
O	CYS150
O	ALA181
O	ASN314
O	TYR318
O	PO4410
O	HOH503
O	HOH530
O	HOH532
O	HOH549
O	HOH554
O	HOH557
O	HOH570
O	HOH580
O	HOH592
O	HOH602
R	EDO404

site_id	AD1
Number of Residues	5
Details	binding site for residue PO4 O 410

Chain	Residue
O	THR180
O	SER182
O	ARG232
O	NAD409
O	HOH557

site_id	AD2
Number of Residues	4
Details	binding site for residue EDO R 401

Chain	Residue
R	ARG19
R	TYR316
R	HOH529
R	HOH533

site_id	AD3
Number of Residues	3
Details	binding site for residue EDO R 402

Chain	Residue
Q	ASP278
Q	LYS296
R	ARG195

site_id	AD4
Number of Residues	5
Details	binding site for residue EDO R 403

Chain	Residue
R	NAD411
R	PO4412
R	HOH501
R	HOH510
R	HOH538

site_id	AD5
Number of Residues	3
Details	binding site for residue EDO R 404

Chain	Residue
O	ALA181
O	NAD409
O	HOH525

site_id	AD6
Number of Residues	5
Details	binding site for residue EDO R 405

Chain	Residue
R	PRO128
R	MET129
R	ASN135
R	LYS217
R	HOH512

site_id	AD7
Number of Residues	4
Details	binding site for residue EDO R 406

Chain	Residue
R	VAL134
R	ASN135
R	GLU136
R	ASP137

site_id	AD8
Number of Residues	4
Details	binding site for residue EDO R 407

Chain	Residue
R	ARG320
R	ARG321
R	ASP324
R	HOH543

site_id	AD9
Number of Residues	3
Details	binding site for residue EDO R 408

Chain	Residue
Q	ASP193
Q	TRP194
R	ASP278

site_id	AE1
Number of Residues	3
Details	binding site for residue GOL R 409

Chain	Residue
R	LYS116
R	ASN143
R	HOH601

site_id	AE2
Number of Residues	4
Details	binding site for residue PEG R 410

Chain	Residue
R	SER149
R	THR151
R	THR209
R	GLY210

site_id	AE3
Number of Residues	33
Details	binding site for residue NAD R 411

Chain	Residue
O	PRO189
R	ASN8
R	GLY9
R	PHE10
R	GLY11
R	ARG12
R	ILE13
R	ASP34
R	PRO35
R	PHE36
R	ARG79
R	SER97
R	THR98
R	GLY99
R	PHE101
R	SER121
R	ALA122
R	ALA181
R	ASN314
R	TYR318
R	EDO403
R	PO4412
R	HOH501
R	HOH514
R	HOH535
R	HOH547
R	HOH551
R	HOH553
R	HOH556
R	HOH557
R	HOH559
R	HOH621
R	HOH628

site_id	AE4
Number of Residues	6
Details	binding site for residue PO4 R 412

Chain	Residue
R	THR180
R	SER182
R	ARG232
R	EDO403
R	NAD411
R	HOH501

site_id	AE5
Number of Residues	2
Details	binding site for residue EDO P 401

Chain	Residue
P	LYS257
P	LYS296

site_id	AE6
Number of Residues	3
Details	binding site for residue EDO P 402

Chain	Residue
P	GLY270
P	PRO288
P	ARG321

site_id	AE7
Number of Residues	5
Details	binding site for residue EDO P 403

Chain	Residue
P	THR98
P	SER182
P	NAD408
P	PO4410
P	HOH510

site_id	AE8
Number of Residues	4
Details	binding site for residue EDO P 404

Chain	Residue
P	GLY133
P	ASN135
P	GLU136
P	ASP137

site_id	AE9
Number of Residues	4
Details	binding site for residue EDO P 405

Chain	Residue
P	THR292
P	HOH523
P	HOH537
R	TYR48

site_id	AF1
Number of Residues	4
Details	binding site for residue EDO P 406

Chain	Residue
O	ASP193
O	TRP194
P	ASP278
P	LYS296

site_id	AF2
Number of Residues	5
Details	binding site for residue GOL P 407

Chain	Residue
P	PRO128
P	MET129
P	ASN135
P	LYS217
P	HOH512

site_id	AF3
Number of Residues	33
Details	binding site for residue NAD P 408

Chain	Residue
P	ASN8
P	GLY9
P	GLY11
P	ARG12
P	ILE13
P	ASN33
P	ASP34
P	PRO35
P	PHE36
P	GLU78
P	ARG79
P	SER97
P	THR98
P	GLY99
P	PHE101
P	SER121
P	ALA122
P	ALA181
P	ASN314
P	TYR318
P	EDO403
P	PO4410
P	HOH511
P	HOH517
P	HOH522
P	HOH526
P	HOH532
P	HOH544
P	HOH561
P	HOH577
P	HOH605
P	HOH614
P	HOH627

site_id	AF4
Number of Residues	4
Details	binding site for residue PO4 P 409

Chain	Residue
P	THR209
P	GLY210
P	ALA211
P	HOH611

site_id	AF5
Number of Residues	7
Details	binding site for residue PO4 P 410

Chain	Residue
P	THR180
P	SER182
P	LYS192
P	ARG232
P	EDO403
P	NAD408
P	HOH510

site_id	AF6
Number of Residues	5
Details	binding site for residue EDO Q 401

Chain	Residue
Q	GLY133
Q	VAL134
Q	ASN135
Q	GLU136
Q	ASP137

site_id	AF7
Number of Residues	3
Details	binding site for residue EDO Q 402

Chain	Residue
Q	GLU23
Q	THR286
Q	PRO288

site_id	AF8
Number of Residues	4
Details	binding site for residue EDO Q 403

Chain	Residue
Q	ALA273
Q	TYR274
Q	HOH533
Q	HOH544

site_id	AF9
Number of Residues	2
Details	binding site for residue EDO Q 404

Chain	Residue
Q	NAD408
Q	PO4409

site_id	AG1
Number of Residues	9
Details	binding site for residue GOL Q 405

Chain	Residue
Q	PRO128
Q	MET129
Q	ASN135
Q	LYS217
Q	GOL406
Q	HOH513
Q	HOH522
Q	HOH576
Q	HOH635

site_id	AG2
Number of Residues	7
Details	binding site for residue GOL Q 406

Chain	Residue
O	MET129
O	ASN135
O	LYS217
O	EDO405
Q	GOL405
Q	HOH501
Q	HOH546

site_id	AG3
Number of Residues	3
Details	binding site for residue GOL Q 407

Chain	Residue
Q	THR209
Q	GLY210
Q	HOH607

site_id	AG4
Number of Residues	32
Details	binding site for residue NAD Q 408

Chain	Residue
Q	ASN8
Q	GLY9
Q	PHE10
Q	GLY11
Q	ARG12
Q	ILE13
Q	ASN33
Q	ASP34
Q	PRO35
Q	PHE36
Q	ARG79
Q	SER97
Q	THR98
Q	GLY99
Q	PHE101
Q	SER121
Q	ALA122
Q	ALA181
Q	ASN314
Q	TYR318
Q	EDO404
Q	PO4409
Q	HOH540
Q	HOH567
Q	HOH570
Q	HOH573
Q	HOH586
Q	HOH592
Q	HOH617
Q	HOH624
Q	HOH625
Q	HOH629

site_id	AG5
Number of Residues	5
Details	binding site for residue PO4 Q 409

Chain	Residue
Q	THR180
Q	SER182
Q	ARG232
Q	EDO404
Q	NAD408

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

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