Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6OK4

Crystal Structure of Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Chlamydia trachomatis with bound NAD

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
A	0005737	cellular_component	cytoplasm
A	0006006	biological_process	glucose metabolic process
A	0006096	biological_process	glycolytic process
A	0016491	molecular_function	oxidoreductase activity
A	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A	0050661	molecular_function	NADP binding
A	0051287	molecular_function	NAD binding
B	0000166	molecular_function	nucleotide binding
B	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
B	0005737	cellular_component	cytoplasm
B	0006006	biological_process	glucose metabolic process
B	0006096	biological_process	glycolytic process
B	0016491	molecular_function	oxidoreductase activity
B	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B	0050661	molecular_function	NADP binding
B	0051287	molecular_function	NAD binding
C	0000166	molecular_function	nucleotide binding
C	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
C	0005737	cellular_component	cytoplasm
C	0006006	biological_process	glucose metabolic process
C	0006096	biological_process	glycolytic process
C	0016491	molecular_function	oxidoreductase activity
C	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C	0050661	molecular_function	NADP binding
C	0051287	molecular_function	NAD binding
D	0000166	molecular_function	nucleotide binding
D	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
D	0005737	cellular_component	cytoplasm
D	0006006	biological_process	glucose metabolic process
D	0006096	biological_process	glycolytic process
D	0016491	molecular_function	oxidoreductase activity
D	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D	0050661	molecular_function	NADP binding
D	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	27
Details	binding site for residue NAD A 401

Chain	Residue
A	GLY7
A	THR96
A	GLY97
A	LEU98
A	THR119
A	ALA120
A	CYS150
A	ALA181
A	ASN314
A	TYR318
A	HOH507
A	PHE8
A	HOH519
A	HOH538
A	HOH543
A	HOH549
A	HOH561
A	HOH571
A	HOH576
C	HOH514
A	GLY9
A	ARG10
A	ILE11
A	ASN32
A	ASP33
A	LEU34
A	SER95

site_id	AC2
Number of Residues	2
Details	binding site for residue EDO A 402

Chain	Residue
A	THR128
A	ASN134

site_id	AC3
Number of Residues	5
Details	binding site for residue EDO A 403

Chain	Residue
A	LYS246
A	HOH539
B	GLU170
C	ARG304
C	EDO404

site_id	AC4
Number of Residues	8
Details	binding site for residue PO4 A 404

Chain	Residue
A	SER149
A	THR151
A	THR209
A	GLY210
A	ALA211
A	HOH509
A	HOH530
A	HOH537

site_id	AC5
Number of Residues	8
Details	binding site for residue PO4 A 405

Chain	Residue
A	GLU170
A	LYS246
A	ARG304
A	HOH559
B	LYS246
C	GLU169
C	ARG304
C	PO4407

site_id	AC6
Number of Residues	5
Details	binding site for residue EDO A 406

Chain	Residue
A	THR49
A	ILE285
C	HOH569
D	THR49
D	ILE285

site_id	AC7
Number of Residues	6
Details	binding site for residue PEG A 407

Chain	Residue
A	GLY132
A	VAL133
A	ASN134
A	HIS135
A	GLN136
A	GLN137

site_id	AC8
Number of Residues	2
Details	binding site for residue CL A 408

Chain	Residue
A	HIS-1
A	HIS0

site_id	AC9
Number of Residues	21
Details	binding site for residue NAD B 401

Chain	Residue
B	GLY7
B	GLY9
B	ARG10
B	ILE11
B	ASN32
B	ASP33
B	LEU34
B	SER95
B	THR96
B	GLY97
B	LEU98
B	THR119
B	ALA120
B	CYS150
B	ALA181
B	ASN314
B	TYR318
B	HOH534
B	HOH536
B	HOH553
D	HOH542

site_id	AD1
Number of Residues	5
Details	binding site for residue EDO B 402

Chain	Residue
B	ASN165
B	ALA259
B	HIS262
B	ALA263
B	HOH540

site_id	AD2
Number of Residues	6
Details	binding site for residue EDO B 403

Chain	Residue
B	LEU163
B	GLY167
B	ILE168
B	GLU221
B	LYS225
B	SER248

site_id	AD3
Number of Residues	8
Details	binding site for residue EDO B 404

Chain	Residue
B	HOH504
C	ASP164
C	ASN165
C	PHE166
B	SER248
B	SER249
B	ALA250
B	ARG304

site_id	AD4
Number of Residues	2
Details	binding site for residue EDO B 405

Chain	Residue
B	TYR253
B	GLY298

site_id	AD5
Number of Residues	5
Details	binding site for residue EDO B 406

Chain	Residue
A	GLN296
B	ASP193
B	ARG195
B	HOH503
B	HOH561

site_id	AD6
Number of Residues	6
Details	binding site for residue PO4 B 407

Chain	Residue
B	SER149
B	THR151
B	THR209
B	GLY210
B	ALA211
B	HOH545

site_id	AD7
Number of Residues	5
Details	binding site for residue PEG B 408

Chain	Residue
B	VAL133
B	ASN134
B	HIS135
B	GLN136
B	GLN137

site_id	AD8
Number of Residues	24
Details	binding site for residue NAD C 401

Chain	Residue
C	GLY7
C	PHE8
C	GLY9
C	ARG10
C	ILE11
C	ASN32
C	ASP33
C	LEU34
C	SER95
C	THR96
C	GLY97
C	LEU98
C	THR119
C	ALA120
C	CYS150
C	ALA181
C	ASN314
C	TYR318
C	HOH506
C	HOH526
C	HOH542
C	HOH549
C	HOH557
C	HOH561

site_id	AD9
Number of Residues	4
Details	binding site for residue EDO C 402

Chain	Residue
A	VAL35
C	PRO189
C	SER190
C	ARG191

site_id	AE1
Number of Residues	3
Details	binding site for residue EDO C 403

Chain	Residue
C	ASP193
C	TRP194
C	HOH545

site_id	AE2
Number of Residues	5
Details	binding site for residue EDO C 404

Chain	Residue
A	ARG304
A	EDO403
C	LYS246
C	ASP303
C	ARG304

site_id	AE3
Number of Residues	1
Details	binding site for residue EDO C 405

Chain	Residue
C	GLN296

site_id	AE4
Number of Residues	6
Details	binding site for residue PO4 C 406

Chain	Residue
C	SER149
C	THR151
C	THR209
C	GLY210
C	ALA211
C	HOH518

site_id	AE5
Number of Residues	7
Details	binding site for residue PO4 C 407

Chain	Residue
A	GLU169
A	ARG304
A	PO4405
C	GLU170
C	LYS246
C	ARG304
D	LYS246

site_id	AE6
Number of Residues	1
Details	binding site for residue EDO C 408

Chain	Residue
C	ALA300

site_id	AE7
Number of Residues	6
Details	binding site for residue PEG C 409

Chain	Residue
C	GLY132
C	VAL133
C	ASN134
C	HIS135
C	GLN136
C	GLN137

site_id	AE8
Number of Residues	21
Details	binding site for residue NAD D 401

Chain	Residue
D	GLY7
D	PHE8
D	GLY9
D	ARG10
D	ILE11
D	ASP33
D	LEU34
D	SER95
D	THR96
D	GLY97
D	LEU98
D	THR119
D	ALA120
D	CYS150
D	ALA181
D	ASN314
D	TYR318
D	HOH510
D	HOH533
D	HOH543
D	HOH583

site_id	AE9
Number of Residues	2
Details	binding site for residue EDO D 402

Chain	Residue
D	THR128
D	ASN134

site_id	AF1
Number of Residues	8
Details	binding site for residue EDO D 403

Chain	Residue
A	ASP164
A	ASN165
A	PHE166
D	SER248
D	SER249
D	ALA250
D	ARG304
D	HOH560

site_id	AF2
Number of Residues	7
Details	binding site for residue PO4 D 404

Chain	Residue
D	SER149
D	THR151
D	THR209
D	GLY210
D	ALA211
D	HOH503
D	HOH538

site_id	AF3
Number of Residues	5
Details	binding site for residue PEG D 405

Chain	Residue
D	VAL133
D	ASN134
D	HIS135
D	GLN136
D	GLN137

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ALA148-LEU155

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"P00362","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	40
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00362","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Site: {"description":"Activates thiol group during catalysis","evidences":[{"source":"UniProtKB","id":"P00362","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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