Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3U33

Crystal Structure of the E. coli adaptive response protein AidB in the space group P3(2)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003677	molecular_function	DNA binding
A	0003995	molecular_function	acyl-CoA dehydrogenase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0006974	biological_process	DNA damage response
A	0008470	molecular_function	3-methylbutanoyl-CoA dehydrogenase activity
A	0016491	molecular_function	oxidoreductase activity
A	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
A	0042802	molecular_function	identical protein binding
A	0043565	molecular_function	sequence-specific DNA binding
A	0045892	biological_process	negative regulation of DNA-templated transcription
B	0003677	molecular_function	DNA binding
B	0003995	molecular_function	acyl-CoA dehydrogenase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0006974	biological_process	DNA damage response
B	0008470	molecular_function	3-methylbutanoyl-CoA dehydrogenase activity
B	0016491	molecular_function	oxidoreductase activity
B	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
B	0042802	molecular_function	identical protein binding
B	0043565	molecular_function	sequence-specific DNA binding
B	0045892	biological_process	negative regulation of DNA-templated transcription
C	0003677	molecular_function	DNA binding
C	0003995	molecular_function	acyl-CoA dehydrogenase activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0006974	biological_process	DNA damage response
C	0008470	molecular_function	3-methylbutanoyl-CoA dehydrogenase activity
C	0016491	molecular_function	oxidoreductase activity
C	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
C	0042802	molecular_function	identical protein binding
C	0043565	molecular_function	sequence-specific DNA binding
C	0045892	biological_process	negative regulation of DNA-templated transcription
D	0003677	molecular_function	DNA binding
D	0003995	molecular_function	acyl-CoA dehydrogenase activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0006974	biological_process	DNA damage response
D	0008470	molecular_function	3-methylbutanoyl-CoA dehydrogenase activity
D	0016491	molecular_function	oxidoreductase activity
D	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
D	0042802	molecular_function	identical protein binding
D	0043565	molecular_function	sequence-specific DNA binding
D	0045892	biological_process	negative regulation of DNA-templated transcription
E	0003677	molecular_function	DNA binding
E	0003995	molecular_function	acyl-CoA dehydrogenase activity
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0006974	biological_process	DNA damage response
E	0008470	molecular_function	3-methylbutanoyl-CoA dehydrogenase activity
E	0016491	molecular_function	oxidoreductase activity
E	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
E	0042802	molecular_function	identical protein binding
E	0043565	molecular_function	sequence-specific DNA binding
E	0045892	biological_process	negative regulation of DNA-templated transcription
F	0003677	molecular_function	DNA binding
F	0003995	molecular_function	acyl-CoA dehydrogenase activity
F	0005515	molecular_function	protein binding
F	0005737	cellular_component	cytoplasm
F	0006974	biological_process	DNA damage response
F	0008470	molecular_function	3-methylbutanoyl-CoA dehydrogenase activity
F	0016491	molecular_function	oxidoreductase activity
F	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
F	0042802	molecular_function	identical protein binding
F	0043565	molecular_function	sequence-specific DNA binding
F	0045892	biological_process	negative regulation of DNA-templated transcription
G	0003677	molecular_function	DNA binding
G	0003995	molecular_function	acyl-CoA dehydrogenase activity
G	0005515	molecular_function	protein binding
G	0005737	cellular_component	cytoplasm
G	0006974	biological_process	DNA damage response
G	0008470	molecular_function	3-methylbutanoyl-CoA dehydrogenase activity
G	0016491	molecular_function	oxidoreductase activity
G	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
G	0042802	molecular_function	identical protein binding
G	0043565	molecular_function	sequence-specific DNA binding
G	0045892	biological_process	negative regulation of DNA-templated transcription
H	0003677	molecular_function	DNA binding
H	0003995	molecular_function	acyl-CoA dehydrogenase activity
H	0005515	molecular_function	protein binding
H	0005737	cellular_component	cytoplasm
H	0006974	biological_process	DNA damage response
H	0008470	molecular_function	3-methylbutanoyl-CoA dehydrogenase activity
H	0016491	molecular_function	oxidoreductase activity
H	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
H	0042802	molecular_function	identical protein binding
H	0043565	molecular_function	sequence-specific DNA binding
H	0045892	biological_process	negative regulation of DNA-templated transcription
I	0003677	molecular_function	DNA binding
I	0003995	molecular_function	acyl-CoA dehydrogenase activity
I	0005515	molecular_function	protein binding
I	0005737	cellular_component	cytoplasm
I	0006974	biological_process	DNA damage response
I	0008470	molecular_function	3-methylbutanoyl-CoA dehydrogenase activity
I	0016491	molecular_function	oxidoreductase activity
I	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
I	0042802	molecular_function	identical protein binding
I	0043565	molecular_function	sequence-specific DNA binding
I	0045892	biological_process	negative regulation of DNA-templated transcription
J	0003677	molecular_function	DNA binding
J	0003995	molecular_function	acyl-CoA dehydrogenase activity
J	0005515	molecular_function	protein binding
J	0005737	cellular_component	cytoplasm
J	0006974	biological_process	DNA damage response
J	0008470	molecular_function	3-methylbutanoyl-CoA dehydrogenase activity
J	0016491	molecular_function	oxidoreductase activity
J	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
J	0042802	molecular_function	identical protein binding
J	0043565	molecular_function	sequence-specific DNA binding
J	0045892	biological_process	negative regulation of DNA-templated transcription
K	0003677	molecular_function	DNA binding
K	0003995	molecular_function	acyl-CoA dehydrogenase activity
K	0005515	molecular_function	protein binding
K	0005737	cellular_component	cytoplasm
K	0006974	biological_process	DNA damage response
K	0008470	molecular_function	3-methylbutanoyl-CoA dehydrogenase activity
K	0016491	molecular_function	oxidoreductase activity
K	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
K	0042802	molecular_function	identical protein binding
K	0043565	molecular_function	sequence-specific DNA binding
K	0045892	biological_process	negative regulation of DNA-templated transcription
L	0003677	molecular_function	DNA binding
L	0003995	molecular_function	acyl-CoA dehydrogenase activity
L	0005515	molecular_function	protein binding
L	0005737	cellular_component	cytoplasm
L	0006974	biological_process	DNA damage response
L	0008470	molecular_function	3-methylbutanoyl-CoA dehydrogenase activity
L	0016491	molecular_function	oxidoreductase activity
L	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
L	0042802	molecular_function	identical protein binding
L	0043565	molecular_function	sequence-specific DNA binding
L	0045892	biological_process	negative regulation of DNA-templated transcription

Functional Information from PDB Data

site_id	AC1
Number of Residues	32
Details	BINDING SITE FOR RESIDUE FAD A 1000

Chain	Residue
A	MET182
A	SER268
A	VAL420
A	ILE423
A	TRP424
A	GLU425
A	GLY426
A	SER427
A	ASN429
A	ILE430
A	LEU433
A	MET184
A	HOH562
A	HOH568
A	HOH579
B	ARG324
B	PHE327
B	LEU331
B	GLN334
B	GLU398
B	VAL399
B	GLY401
A	THR185
B	GLY402
B	HOH565
B	HOH572
A	GLY189
A	GLY190
A	SER191
A	PHE216
A	SER218
A	LYS260

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 542

Chain	Residue
A	ARG71
A	TYR72
D	ARG256

site_id	AC3
Number of Residues	32
Details	BINDING SITE FOR RESIDUE FAD B 1000

Chain	Residue
A	ARG324
A	VAL326
A	PHE327
A	LEU331
A	GLN334
A	MET337
A	GLU398
A	VAL399
A	GLY402
A	TYR405
A	HOH563
B	MET182
B	MET184
B	THR185
B	GLY189
B	GLY190
B	SER191
B	PHE216
B	SER218
B	LYS260
B	SER268
B	VAL420
B	ILE423
B	TRP424
B	GLU425
B	GLY426
B	SER427
B	ASN429
B	ILE430
B	LEU433
B	HOH566
B	HOH573

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL B 542

Chain	Residue
B	ARG71
B	TYR72
C	ARG256

site_id	AC5
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD C 1000

Chain	Residue
C	MET182
C	MET184
C	THR185
C	GLY189
C	GLY190
C	SER191
C	PHE216
C	SER218
C	LYS260
C	SER268
C	VAL420
C	ILE423
C	TRP424
C	GLU425
C	GLY426
C	SER427
C	ASN429
C	ILE430
C	LEU433
C	HOH564
D	ARG324
D	PHE327
D	LEU331
D	GLN334
D	MET337
D	GLU398
D	VAL399
D	GLY402

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL C 542

Chain	Residue
C	ARG71
C	TYR72
B	ARG256

site_id	AC7
Number of Residues	29
Details	BINDING SITE FOR RESIDUE FAD D 1000

Chain	Residue
C	ARG324
C	VAL326
C	PHE327
C	LEU331
C	GLN334
C	MET337
C	GLU398
C	VAL399
C	GLY401
C	GLY402
D	MET182
D	MET184
D	THR185
D	GLY189
D	GLY190
D	SER191
D	PHE216
D	SER218
D	LYS260
D	SER268
D	VAL420
D	ILE423
D	TRP424
D	GLY426
D	SER427
D	ASN429
D	ILE430
D	LEU433
D	HOH555

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL D 542

Chain	Residue
A	ARG256
D	ARG71
D	TYR72

site_id	AC9
Number of Residues	30
Details	BINDING SITE FOR RESIDUE FAD E 1000

Chain	Residue
E	MET182
E	MET184
E	THR185
E	GLY189
E	GLY190
E	SER191
E	PHE216
E	SER218
E	LYS260
E	ASN263
E	SER268
E	VAL420
E	ILE423
E	TRP424
E	GLU425
E	GLY426
E	SER427
E	ASN429
E	LEU433
E	HOH554
F	ARG324
F	PHE327
F	LEU331
F	GLN334
F	MET337
F	GLU398
F	VAL399
F	GLY401
F	GLY402
F	TYR405

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL E 542

Chain	Residue
E	ARG71
E	TYR72

site_id	BC2
Number of Residues	30
Details	BINDING SITE FOR RESIDUE FAD F 1000

Chain	Residue
E	ARG324
E	PHE327
E	LEU331
E	GLN334
E	MET337
E	GLU398
E	VAL399
E	GLY401
E	GLY402
E	HOH557
F	MET182
F	MET184
F	THR185
F	GLY189
F	GLY190
F	SER191
F	PHE216
F	SER218
F	LYS260
F	SER268
F	VAL420
F	ILE423
F	TRP424
F	GLU425
F	GLY426
F	SER427
F	ASN429
F	ILE430
F	LEU433
F	HOH560

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL F 542

Chain	Residue
F	ARG71
F	TYR72
G	ARG256

site_id	BC4
Number of Residues	27
Details	BINDING SITE FOR RESIDUE FAD G 1000

Chain	Residue
G	MET182
G	MET184
G	THR185
G	GLY189
G	GLY190
G	SER191
G	PHE216
G	SER218
G	LYS260
G	SER268
G	VAL420
G	ILE423
G	GLY426
G	SER427
G	ASN429
G	LEU433
G	HOH561
G	HOH565
H	ARG324
H	VAL326
H	PHE327
H	LEU331
H	MET337
H	GLU398
H	VAL399
H	GLY401
H	GLY402

site_id	BC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL G 542

Chain	Residue
F	ARG256
G	ARG71

site_id	BC6
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD H 1000

Chain	Residue
G	ARG324
G	VAL326
G	PHE327
G	LEU331
G	GLN334
G	MET337
G	GLU398
G	VAL399
G	GLY401
G	GLY402
H	MET182
H	MET184
H	THR185
H	GLY189
H	GLY190
H	SER191
H	PHE216
H	SER218
H	LYS260
H	SER268
H	VAL420
H	ILE423
H	TRP424
H	GLY426
H	SER427
H	ASN429
H	ILE430
H	LEU433

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL H 542

Chain	Residue
E	ARG256
H	ARG71
H	TYR72

site_id	BC8
Number of Residues	30
Details	BINDING SITE FOR RESIDUE FAD I 1000

Chain	Residue
I	MET182
I	MET184
I	THR185
I	GLY189
I	GLY190
I	SER191
I	PHE216
I	SER218
I	LYS260
I	ASN263
I	SER268
I	VAL420
I	ILE423
I	TRP424
I	GLU425
I	GLY426
I	SER427
I	ASN429
J	ARG324
J	VAL326
J	PHE327
J	LEU331
J	GLN334
J	MET337
J	GLU398
J	VAL399
J	GLY401
J	GLY402
J	TYR405
J	HOH549

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL I 542

Chain	Residue
I	ARG71
I	TYR72
L	ARG256

site_id	CC1
Number of Residues	26
Details	BINDING SITE FOR RESIDUE FAD J 1000

Chain	Residue
I	ARG324
I	VAL326
I	PHE327
I	LEU331
I	GLN334
I	MET337
I	GLU398
I	VAL399
I	GLY402
J	MET182
J	MET184
J	THR185
J	GLY189
J	GLY190
J	SER191
J	PHE216
J	SER218
J	LYS260
J	SER268
J	VAL420
J	ILE423
J	GLY426
J	SER427
J	ASN429
J	ILE430
J	LEU433

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL J 542

Chain	Residue
J	LEU69
J	LEU70
J	ARG71
J	TYR72
K	ARG256

site_id	CC3
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD K 1000

Chain	Residue
K	MET182
K	MET184
K	THR185
K	GLY189
K	GLY190
K	SER191
K	PHE216
K	SER218
K	LYS260
K	SER268
K	VAL420
K	ILE423
K	GLU425
K	GLY426
K	SER427
K	ASN429
K	LEU433
K	HOH559
L	ARG324
L	VAL326
L	PHE327
L	LEU331
L	GLN334
L	MET337
L	GLU398
L	VAL399
L	GLY401
L	GLY402

site_id	CC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL K 542

Chain	Residue
J	ARG256
K	ARG71
K	TYR72

site_id	CC5
Number of Residues	29
Details	BINDING SITE FOR RESIDUE FAD L 1000

Chain	Residue
K	ARG324
K	VAL326
K	PHE327
K	LEU331
K	GLN334
K	MET337
K	GLU398
K	VAL399
K	GLY402
K	HOH558
L	MET182
L	MET184
L	THR185
L	GLY189
L	GLY190
L	SER191
L	PHE216
L	SER218
L	LYS260
L	SER268
L	VAL420
L	ILE423
L	TRP424
L	GLU425
L	GLY426
L	SER427
L	ASN429
L	HOH558
L	HOH559

site_id	CC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL L 542

Chain	Residue
I	ARG256
L	ARG71
L	TYR72

Functional Information from PROSITE/UniProt

site_id	PS00072
Number of Residues	13
Details	ACYL_COA_DH_1 Acyl-CoA dehydrogenases signature 1. GMTEkqGGSDvmS

Chain	Residue	Details
A	GLY183-SER195

site_id	PS00073
Number of Residues	20
Details	ACYL_COA_DH_2 Acyl-CoA dehydrogenases signature 2. EvLGGiGYceEselpRlyrE

Chain	Residue	Details
A	GLU398-GLU417

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	300
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18829440","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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