Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2WOX

Betaine aldehyde dehydrogenase from Pseudomonas aeruginosa with NAD(P) H-catalytic thiol adduct.

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NDP A 1491

Chain	Residue
A	ILE149
A	GLY213
A	GLN214
A	PHE227
A	THR228
A	GLY229
A	GLY230
A	THR233
A	VAL237
A	GLU252
A	LEU253
A	GLY150
A	GLY254
A	CYS286
A	GLU387
A	PHE389
A	7PE1496
A	HOH2223
A	TRP152
A	ASN153
A	LYS176
A	SER178
A	GLU179
A	SER208
A	GLY209

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K A 1492

Chain	Residue
A	THR26
A	ILE27
A	ASP93
A	VAL180

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K A 1493

Chain	Residue
A	LYS457
A	GLY460
B	LEU246
B	HOH2185

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 1494

Chain	Residue
A	TRP161
A	GLU252
A	SER447
A	GLU464
A	7PE1496

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BME A 1600

Chain	Residue
A	LEU307
A	GLN311
A	LEU352
A	CYS353

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL B 1490

Chain	Residue
B	ARG210
B	NDP1491

site_id	AC7
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NDP B 1491

Chain	Residue
B	ILE149
B	GLY150
B	TRP152
B	ASN153
B	LYS176
B	SER178
B	GLU179
B	GLY207
B	SER208
B	GLY209
B	GLY213
B	PHE227
B	THR228
B	GLY229
B	GLY230
B	THR233
B	GLU252
B	LEU253
B	GLY254
B	CYS286
B	GLU387
B	PHE389
B	LEU415
B	GOL1490
B	GOL1495
B	HOH2163
B	HOH2195
B	HOH2258
B	HOH2259
B	HOH2260

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K B 1493

Chain	Residue
A	LEU246
B	LYS457
B	GLY460

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 1495

Chain	Residue
B	TRP161
B	GLU252
B	CYS286
B	SER447
B	VAL453
B	GLU464
B	NDP1491
B	HOH2196

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL B 1496

Chain	Residue
B	ALA61
B	MET63
B	ALA65
B	ARG68
B	HOH2262
B	HOH2263
B	HOH2264
B	HOH2265
D	HOH2106

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 1497

Chain	Residue
B	PHE4
B	GLN7
B	LYS187
B	GOL1498
B	HOH2002

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 1498

Chain	Residue
B	GLU5
B	GLN7
B	LYS8
B	TYR15
B	GOL1497

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 7PE B 1499

Chain	Residue
B	GLY12
B	SER52
B	GLU55
B	ILE71
B	GLY196
B	PRO198
B	ASP199

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K B 1501

Chain	Residue
B	THR26
B	ILE27
B	ASP93
B	VAL180

site_id	BC6
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NDP C 1491

Chain	Residue
C	ILE149
C	GLY150
C	ALA151
C	TRP152
C	ASN153
C	LYS176
C	SER178
C	GLU179
C	SER208
C	GLY209
C	ARG210
C	GLY213
C	PHE227
C	THR228
C	GLY229
C	GLY230
C	THR233
C	LYS236
C	VAL237
C	GLU252
C	LEU253
C	GLY254
C	CYS286
C	GLU387
C	PHE389
C	LEU415
C	GOL1497
C	HOH2352
C	HOH2353
C	HOH2354
C	HOH2355

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K C 1492

Chain	Residue
C	THR26
C	ILE27
C	ASP93
C	VAL180

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K C 1493

Chain	Residue
C	LYS457
C	GLY460
D	LEU246
D	HOH2147

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL C 1495

Chain	Residue
C	PHE4
C	GLN7
C	LYS187

site_id	CC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL C 1496

Chain	Residue
C	TYR154
C	GLN157
C	CYS286
C	GOL1497
C	GOL1499
C	HOH2356
C	HOH2357
C	HOH2358

site_id	CC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 1497

Chain	Residue
C	TRP161
C	GLU252
C	GLU464
C	NDP1491
C	GOL1496
C	HOH2338

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 1498

Chain	Residue
C	ARG314
C	LEU315
C	ASP320
C	THR323

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 1499

Chain	Residue
C	SER447
C	GOL1496
C	7PE1501
C	HOH2128
C	HOH2360

site_id	CC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL C 1500

Chain	Residue
C	SER336
C	GLY339
C	TYR340

site_id	CC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BME C 1600

Chain	Residue
C	LEU307
C	GLN311
C	LEU352
C	CYS353
C	HOH2119

site_id	CC7
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NDP D 1491

Chain	Residue
D	ILE149
D	GLY150
D	TRP152
D	ASN153
D	LYS176
D	SER178
D	GLU179
D	GLY207
D	GLY209
D	PHE227
D	THR228
D	GLY229
D	GLY230
D	THR233
D	VAL237
D	GLU252
D	LEU253
D	GLY254
D	CYS286
D	GLU387
D	PHE389
D	LEU415
D	GOL1496
D	HOH2235

site_id	CC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K D 1492

Chain	Residue
D	THR26
D	ILE27
D	ASP93
D	VAL180

site_id	CC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K D 1493

Chain	Residue
C	LEU246
C	HOH2203
D	LYS457
D	GLY460

site_id	DC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 1494

Chain	Residue
D	GLU5
D	GLU6
D	GLN7
D	LYS8
D	TYR15
D	GOL1497

site_id	DC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D 1495

Chain	Residue
D	GLN157
D	CYS286
D	GOL1496
D	HOH2165
D	HOH2235

site_id	DC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 1496

Chain	Residue
D	GLU252
D	CYS286
D	SER447
D	NDP1491
D	GOL1495
D	HOH2165

site_id	DC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D 1497

Chain	Residue
D	PHE4
D	GLU5
D	GLN7
D	LYS187
D	GOL1494

site_id	DC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE 7PE A 1495

Chain	Residue
A	ALA122
A	ARG140
A	ALA471
D	ALA122

site_id	DC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 7PE A 1496

Chain	Residue
A	TYR154
A	GLN157
A	TRP161
A	NDP1491
A	GOL1494
A	HOH2214
A	HOH2224

site_id	DC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE 7PE B 1500

Chain	Residue
B	GLN157
B	GLY445
B	SER447

site_id	DC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 7PE C 1501

Chain	Residue
C	MET276
C	PHE280
C	THR287
C	ASN288
C	TRP444
C	GLY445
C	GOL1499
C	HOH2361
C	HOH2362
C	HOH2363
D	TYR486
D	ALA487
D	HOH2228

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	8
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	4
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	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"21732915","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	28
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	44
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	4
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	4
Details	Site: {"description":"Seems to be a necessary countercharge to the potassium cations"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
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)