Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6BPG

Crystal structure of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa with bound rubidium ions

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008802	molecular_function	betaine-aldehyde 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	0019285	biological_process	glycine betaine biosynthetic process from choline
A	0046872	molecular_function	metal ion binding
B	0008802	molecular_function	betaine-aldehyde 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	0019285	biological_process	glycine betaine biosynthetic process from choline
B	0046872	molecular_function	metal ion binding
C	0008802	molecular_function	betaine-aldehyde 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	0019285	biological_process	glycine betaine biosynthetic process from choline
C	0046872	molecular_function	metal ion binding
D	0008802	molecular_function	betaine-aldehyde 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	0019285	biological_process	glycine betaine biosynthetic process from choline
D	0046872	molecular_function	metal ion binding
E	0008802	molecular_function	betaine-aldehyde dehydrogenase (NAD+) activity
E	0016491	molecular_function	oxidoreductase activity
E	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
E	0019285	biological_process	glycine betaine biosynthetic process from choline
E	0046872	molecular_function	metal ion binding
F	0008802	molecular_function	betaine-aldehyde dehydrogenase (NAD+) activity
F	0016491	molecular_function	oxidoreductase activity
F	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
F	0019285	biological_process	glycine betaine biosynthetic process from choline
F	0046872	molecular_function	metal ion binding
G	0008802	molecular_function	betaine-aldehyde dehydrogenase (NAD+) activity
G	0016491	molecular_function	oxidoreductase activity
G	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
G	0019285	biological_process	glycine betaine biosynthetic process from choline
G	0046872	molecular_function	metal ion binding
H	0008802	molecular_function	betaine-aldehyde dehydrogenase (NAD+) activity
H	0016491	molecular_function	oxidoreductase activity
H	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
H	0019285	biological_process	glycine betaine biosynthetic process from choline
H	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue RB A 501

Chain	Residue
A	THR26
A	ILE27
A	ASP93
A	VAL180

site_id	AC2
Number of Residues	5
Details	binding site for residue RB A 502

Chain	Residue
A	LYS457
A	GLY460
A	VAL461
B	LEU246
B	GLU248

site_id	AC3
Number of Residues	3
Details	binding site for residue RB B 501

Chain	Residue
A	LEU246
B	LYS457
B	GLY460

site_id	AC4
Number of Residues	4
Details	binding site for residue RB B 502

Chain	Residue
B	THR26
B	ILE27
B	ASP93
B	VAL180

site_id	AC5
Number of Residues	4
Details	binding site for residue RB C 501

Chain	Residue
C	LYS457
C	GLY460
D	GLU223
D	LEU246

site_id	AC6
Number of Residues	4
Details	binding site for residue RB C 502

Chain	Residue
C	THR26
C	ILE27
C	ASP93
C	VAL180

site_id	AC7
Number of Residues	4
Details	binding site for residue RB D 501

Chain	Residue
C	GLU223
C	LEU246
D	LYS457
D	GLY460

site_id	AC8
Number of Residues	4
Details	binding site for residue RB D 502

Chain	Residue
D	THR26
D	ILE27
D	ASP93
D	VAL180

site_id	AC9
Number of Residues	4
Details	binding site for residue RB E 501

Chain	Residue
E	LYS457
E	GLY460
F	GLU223
F	LEU246

site_id	AD1
Number of Residues	4
Details	binding site for residue RB E 502

Chain	Residue
E	THR26
E	ILE27
E	ASP93
E	VAL180

site_id	AD2
Number of Residues	3
Details	binding site for residue RB F 501

Chain	Residue
E	LEU246
F	LYS457
F	GLY460

site_id	AD3
Number of Residues	4
Details	binding site for residue RB F 502

Chain	Residue
F	THR26
F	ILE27
F	ASP93
F	VAL180

site_id	AD4
Number of Residues	4
Details	binding site for residue RB G 501

Chain	Residue
G	THR26
G	ILE27
G	ASP93
G	VAL180

site_id	AD5
Number of Residues	4
Details	binding site for residue RB G 502

Chain	Residue
G	LYS457
G	GLY460
H	LEU246
H	GLU248

site_id	AD6
Number of Residues	6
Details	binding site for residue RB G 503

Chain	Residue
G	GLU223
G	LEU246
G	GLU248
H	LYS457
H	GLY460
H	VAL461

site_id	AD7
Number of Residues	4
Details	binding site for residue RB H 501

Chain	Residue
H	THR26
H	ILE27
H	ASP93
H	VAL180

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE279-THR290

site_id	PS00687
Number of Residues	8
Details	ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. MELGGKSP

Chain	Residue	Details
A	MET251-PRO258

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"HAMAP-Rule","id":"MF_00804","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19013472","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00804","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19013472","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"21732915","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	56
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	88
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21732915","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2WOX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"21732915","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2WOX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	8
Details	Site: {"description":"Seems to be a necessary countercharge to the potassium cations"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	8
Details	Modified residue: {"description":"Cysteine sulfenic acid (-SOH)","evidences":[{"source":"HAMAP-Rule","id":"MF_00804","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19013472","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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