Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2XDR

CRYSTALLOGRAPHIC STRUCTURE OF BETAINE ALDEHYDE DEHYDROGENASE MUTANT E252A FROM PSEUDOMONAS AERUGINOSA

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	8
Details	BINDING SITE FOR RESIDUE GOL A 1491

Chain	Residue
A	ILE438
A	SER447
A	VAL453
A	GLU464
A	TOE1492
A	HOH2530
A	HOH2531
A	HOH2534

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TOE A 1492

Chain	Residue
A	ILE158
A	SER447
A	GOL1491
A	HOH2086
A	HOH2259
A	HOH2309
A	HOH2342
A	HOH2532
A	HOH2533
A	HOH2534
A	GLN157

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

Chain	Residue
A	THR26
A	ILE27
A	ASP93
A	VAL180

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K A 1494

Chain	Residue
A	LYS457
A	GLY460
B	LEU246

site_id	AC5
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NDP A 5502

Chain	Residue
A	ILE149
A	GLY150
A	LYS176
A	SER178
A	GLU179
A	SER208
A	GLY209
A	GLY213
A	GLN214
A	PHE227
A	GLY230
A	THR233
A	VAL237
A	HOH2296
A	HOH2536
A	HOH2537
A	HOH2538
A	HOH2540
A	HOH2541
A	HOH2542
A	HOH2543
A	HOH2544
A	HOH2545

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL B 1491

Chain	Residue
B	CYS286
B	ILE438
B	SER447
B	VAL453
B	GLU464
B	GOL1492
B	HOH2351
B	HOH2355
B	HOH2381
B	HOH2383

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 1492

Chain	Residue
B	TYR154
B	GLN157
B	GOL1491
B	HOH2382
B	HOH2383

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 1493

Chain	Residue
B	PHE4
B	GLN7
B	LYS187
B	HOH2007
B	HOH2014
B	HOH2384

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 1494

Chain	Residue
B	GLU5
B	GLU6
B	GLN7
B	LYS8
B	TYR15
B	HOH2384

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K B 5500

Chain	Residue
A	LEU246
B	LYS457
B	GLY460

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K B 5501

Chain	Residue
B	THR26
B	ILE27
B	ASP93
B	VAL180

site_id	BC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NDP B 5502

Chain	Residue
B	HOH2387
B	HOH2388
B	HOH2390
B	ILE149
B	GLY150
B	LYS176
B	SER178
B	GLU179
B	GLY207
B	GLY209
B	GLY213
B	GLN214
B	PHE227
B	GLY229
B	GLY230
B	THR233
B	VAL237
B	HOH2385
B	HOH2386

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 1491

Chain	Residue
C	PHE4
C	GLN7
C	LYS187
C	HOH2325

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 1492

Chain	Residue
C	GLN157
C	VAL285
C	GOL1493
C	HOH2143
C	HOH2146
C	HOH2326
C	HOH2327

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 1493

Chain	Residue
C	CYS286
C	GLU464
C	GOL1492
C	HOH2174
C	HOH2294
C	HOH2328
C	HOH2329

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 1494

Chain	Residue
C	ARG314
C	LEU315
C	ASP320
C	THR323
C	HOH2330

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL C 1495

Chain	Residue
C	SER336
C	GLY339
C	TYR340

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K C 1496

Chain	Residue
C	THR26
C	ILE27
C	ASP93
C	VAL180

site_id	CC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K C 1497

Chain	Residue
C	LYS457
C	GLY460
D	LEU246

site_id	CC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE NDP C 5502

Chain	Residue
C	ILE149
C	GLY150
C	LYS176
C	SER178
C	GLU179
C	GLY207
C	GLY209
C	GLY213
C	GLN214
C	PHE227
C	GLY229
C	GLY230
C	THR233
C	VAL237
C	HOH2332
C	HOH2333
C	HOH2334
C	HOH2335
C	HOH2336
C	HOH2337

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 1491

Chain	Residue
D	GLU5
D	GLU6
D	GLN7
D	LYS8
D	TYR15
D	HOH2399

site_id	CC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 1492

Chain	Residue
D	GLN157
D	VAL285
D	GOL1493
D	HOH2283
D	HOH2395
D	HOH2396

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D 1493

Chain	Residue
D	CYS286
D	SER447
D	GLU464
D	GOL1492
D	HOH2397

site_id	CC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 1494

Chain	Residue
D	PHE4
D	GLU5
D	GLN7
D	LYS187
D	HOH2398
D	HOH2399

site_id	CC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K D 1495

Chain	Residue
D	THR26
D	ILE27
D	ASP93
D	VAL180

site_id	CC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K D 1496

Chain	Residue
C	LEU246
D	LYS457
D	GLY460

site_id	CC9
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NDP D 5502

Chain	Residue
D	ILE149
D	GLY150
D	LYS176
D	SER178
D	GLU179
D	GLY207
D	SER208
D	GLY209
D	GLY213
D	GLN214
D	PHE227
D	THR228
D	GLY229
D	GLY230
D	THR233
D	VAL237
D	HOH2223
D	HOH2400
D	HOH2401
D	HOH2404
D	HOH2406
D	HOH2407
D	HOH2408
D	HOH2410

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

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)