Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3QV1

Crystal structure of the binary complex of photosyntetic A4 glyceraldehyde 3-phosphate dehydrogenase (GAPDH) with cp12-2, both from Arabidopsis thaliana.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006006	biological_process	glucose metabolic process
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	0006006	biological_process	glucose metabolic process
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	0006006	biological_process	glucose metabolic process
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	0006006	biological_process	glucose metabolic process
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
E	0006006	biological_process	glucose metabolic process
E	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
E	0050661	molecular_function	NADP binding
E	0051287	molecular_function	NAD binding
F	0006006	biological_process	glucose metabolic process
F	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
F	0050661	molecular_function	NADP binding
F	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE NAD A 335

Chain	Residue
A	GLY7
A	GLY97
A	PHE99
A	THR119
A	ALA120
A	ASN313
A	TYR317
A	SO4338
A	HOH342
A	HOH345
A	HOH346
A	GLY9
A	HOH353
A	HOH382
G	GLU72
A	ARG10
A	ILE11
A	ASP32
A	THR33
A	ARG77
A	GLY95
A	THR96

site_id	AC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAD B 335

Chain	Residue
B	GLY7
B	GLY9
B	ARG10
B	ILE11
B	ASN31
B	ASP32
B	THR33
B	ARG77
B	GLY95
B	THR96
B	GLY97
B	THR119
B	ALA120
B	CYS149
B	ASN313
B	TYR317
B	HOH337
B	HOH340
B	HOH344
B	HOH348
B	HOH353
B	HOH361
B	HOH364
H	GLU72

site_id	AC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAD C 335

Chain	Residue
C	GLY7
C	PHE8
C	GLY9
C	ARG10
C	ILE11
C	ASN31
C	ASP32
C	THR33
C	ARG77
C	GLY95
C	THR96
C	GLY97
C	PHE99
C	THR119
C	ALA120
C	ASN313
C	TYR317
C	HOH349
C	HOH350
C	HOH354
C	HOH357
H	GLU69
H	TYR76

site_id	AC4
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAD D 335

Chain	Residue
A	HOH359
D	GLY7
D	GLY9
D	ARG10
D	ILE11
D	ASN31
D	ASP32
D	THR33
D	ARG77
D	GLY95
D	THR96
D	GLY97
D	THR119
D	ALA120
D	CYS149
D	ASN313
D	GLU314
D	TYR317
D	HOH337
D	HOH340
D	HOH345
D	HOH352
D	HOH368
D	HOH370
G	GLU69
G	TYR76

site_id	AC5
Number of Residues	20
Details	BINDING SITE FOR RESIDUE NAD E 335

Chain	Residue
E	ASP32
E	THR33
E	ARG77
E	GLY95
E	THR96
E	GLY97
E	PHE99
E	THR119
E	ALA120
E	CYS149
E	ASN313
E	TYR317
E	HOH338
E	HOH344
E	HOH347
I	GLU72
E	GLY7
E	GLY9
E	ARG10
E	ILE11

site_id	AC6
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NAD F 335

Chain	Residue
F	GLY7
F	PHE8
F	GLY9
F	ARG10
F	ILE11
F	ASN31
F	ASP32
F	THR33
F	ARG77
F	GLY95
F	THR96
F	GLY97
F	THR119
F	ASN313
F	GLU314
F	TYR317
F	HOH336
F	HOH337
F	HOH338
I	GLU69
I	TYR76

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PEG C 334

Chain	Residue
A	THR173
A	THR175
A	ASP241
C	THR173
C	THR175
C	VAL239
C	ASP241

site_id	AC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PEG A 334

Chain	Residue
A	THR171
A	MET172
A	THR173
A	ASP241
A	VAL243
A	LYS306
C	THR171
C	MET172
C	THR173
C	ASP241
C	VAL243
C	LYS306

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PEG A 336

Chain	Residue
A	HOH189
A	ALA200
A	LEU201
A	PRO233
B	LEU201
C	PRO233
C	THR234
C	PRO235
C	ARG284

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 336

Chain	Residue
B	ARG197
C	ASP47
C	GLY51
C	ILE52
D	VAL281
D	ASP282

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 337

Chain	Residue
A	SER148
A	CYS149
A	THR150
A	THR208
A	HOH371

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 338

Chain	Residue
A	THR179
A	ASP181
A	ARG231
A	NAD335

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	ALA147-LEU154

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Nucleophile => ECO:0000255\|PROSITE-ProRule:PRU10009

Chain	Residue	Details
A	CYS149
B	CYS149
C	CYS149
D	CYS149
E	CYS149
F	CYS149

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:20516587, ECO:0000269\|PubMed:22514274

Chain	Residue	Details
A	ARG10
C	ASP32
C	ARG77
C	ASN313
D	ARG10
D	ASP32
D	ARG77
D	ASN313
E	ARG10
E	ASP32
E	ARG77
A	ASP32
E	ASN313
F	ARG10
F	ASP32
F	ARG77
F	ASN313
A	ARG77
A	ASN313
B	ARG10
B	ASP32
B	ARG77
B	ASN313
C	ARG10

site_id	SWS_FT_FI3
Number of Residues	30
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	SER148
B	ARG231
C	SER148
C	THR179
C	ARG195
C	THR208
C	ARG231
D	SER148
D	THR179
D	ARG195
D	THR208
A	THR179
D	ARG231
E	SER148
E	THR179
E	ARG195
E	THR208
E	ARG231
F	SER148
F	THR179
F	ARG195
F	THR208
A	ARG195
F	ARG231
A	THR208
A	ARG231
B	SER148
B	THR179
B	ARG195
B	THR208

site_id	SWS_FT_FI4
Number of Residues	6
Details	SITE: Activates thiol group during catalysis => ECO:0000250

Chain	Residue	Details
A	HIS176
B	HIS176
C	HIS176
D	HIS176
E	HIS176
F	HIS176

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