Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2EUH

HOLO FORM OF A NADP DEPENDENT ALDEHYDE DEHYDROGENASE COMPLEX WITH NADP+

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008886	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity
A	0008911	molecular_function	lactaldehyde dehydrogenase (NAD+) activity
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	0047100	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity
B	0008886	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity
B	0008911	molecular_function	lactaldehyde dehydrogenase (NAD+) activity
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	0047100	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity
C	0008886	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity
C	0008911	molecular_function	lactaldehyde dehydrogenase (NAD+) activity
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	0047100	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity
D	0008886	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity
D	0008911	molecular_function	lactaldehyde dehydrogenase (NAD+) activity
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	0047100	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 477

Chain	Residue
B	ARG103
B	ARG283
B	THR285
B	GLN436
B	ARG437
B	GLY438

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 478

Chain	Residue
C	GLU351
B	ASP327
B	THR328
B	LYS329

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 477

Chain	Residue
C	ARG103
C	ARG283
C	THR285
C	GLN436
C	ARG437
C	GLY438

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 477

Chain	Residue
D	ARG103
D	ARG283
D	THR285
D	GLN436
D	ARG437
D	GLY438

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 478

Chain	Residue
A	GLU351
D	ASP327
D	THR328
D	LYS329

site_id	AC6
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAP A 476

Chain	Residue
A	ILE150
A	SER151
A	PRO152
A	PHE153
A	ASN154
A	LYS177
A	PRO179
A	THR180
A	GLY208
A	ARG209
A	GLY210
A	GLY214
A	ASP215
A	VAL218
A	PHE228
A	THR229
A	GLY230
A	SER231
A	ILE234
A	GLU250
A	LEU251
A	GLY252
A	CYS284
A	GLU377
A	PHE379
A	ARG437
A	PHE444

site_id	AC7
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAP B 476

Chain	Residue
B	ILE150
B	SER151
B	PRO152
B	PHE153
B	ASN154
B	LYS177
B	PRO178
B	PRO179
B	THR180
B	GLY210
B	GLY214
B	ASP215
B	PHE228
B	THR229
B	GLY230
B	SER231
B	ILE234
B	GLU250
B	LEU251
B	GLY252
B	CYS284
B	GLU377
B	PHE379
B	ARG437
B	PHE444
B	HOH522

site_id	AC8
Number of Residues	28
Details	BINDING SITE FOR RESIDUE NAP C 476

Chain	Residue
C	LEU251
C	CYS284
C	GLU377
C	PHE379
C	LEU405
C	ARG437
C	PHE444
C	HOH526
C	ILE150
C	SER151
C	PRO152
C	PHE153
C	ASN154
C	LEU159
C	LYS177
C	PRO178
C	PRO179
C	THR180
C	ARG209
C	GLY210
C	GLY214
C	ASP215
C	PHE228
C	THR229
C	GLY230
C	SER231
C	ILE234
C	GLU250

site_id	AC9
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAP D 476

Chain	Residue
D	ILE150
D	SER151
D	PRO152
D	PHE153
D	ASN154
D	LEU159
D	LYS177
D	PRO178
D	PRO179
D	THR180
D	GLY208
D	ARG209
D	GLY210
D	GLY214
D	ASP215
D	VAL218
D	PHE228
D	THR229
D	GLY230
D	SER231
D	ILE234
D	GLU250
D	LEU251
D	GLY252
D	CYS284
D	GLU377
D	PHE379
D	LEU405
D	ARG437
D	PHE444

Functional Information from PROSITE/UniProt

site_id	PS00070
Number of Residues	12
Details	ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FgYSGQRCTAVK

Chain	Residue	Details
A	PHE277-LYS288

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10864505","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	104
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10388564","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10864505","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16958622","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1a4s

Chain	Residue	Details
A	ASN154
A	CYS284
A	GLU250

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1a4s

Chain	Residue	Details
B	ASN154
B	CYS284
B	GLU250

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1a4s

Chain	Residue	Details
C	ASN154
C	CYS284
C	GLU250

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1a4s

Chain	Residue	Details
D	ASN154
D	CYS284
D	GLU250

site_id	MCSA1
Number of Residues	3
Details	M-CSA 711

Chain	Residue	Details
A	ASN154	electrostatic stabiliser
A	GLU250	activator, electrostatic stabiliser, proton acceptor, proton donor
A	CYS284	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor

site_id	MCSA2
Number of Residues	3
Details	M-CSA 711

Chain	Residue	Details
B	ASN154	electrostatic stabiliser
B	GLU250	activator, electrostatic stabiliser, proton acceptor, proton donor
B	CYS284	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor

site_id	MCSA3
Number of Residues	3
Details	M-CSA 711

Chain	Residue	Details
C	ASN154	electrostatic stabiliser
C	GLU250	activator, electrostatic stabiliser, proton acceptor, proton donor
C	CYS284	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor

site_id	MCSA4
Number of Residues	3
Details	M-CSA 711

Chain	Residue	Details
D	ASN154	electrostatic stabiliser
D	GLU250	activator, electrostatic stabiliser, proton acceptor, proton donor
D	CYS284	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)