Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5G5G

Escherichia coli Periplasmic Aldehyde Oxidase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0005515	molecular_function	protein binding
B	0016491	molecular_function	oxidoreductase activity
B	0016903	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors
B	0030288	cellular_component	outer membrane-bounded periplasmic space
B	0042597	cellular_component	periplasmic space
B	0046872	molecular_function	metal ion binding
B	0047770	molecular_function	carboxylate reductase activity
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	0071949	molecular_function	FAD binding
B	0110095	biological_process	cellular detoxification of aldehyde
B	1990204	cellular_component	oxidoreductase complex
C	0005506	molecular_function	iron ion binding
C	0005515	molecular_function	protein binding
C	0006974	biological_process	DNA damage response
C	0016491	molecular_function	oxidoreductase activity
C	0016903	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors
C	0030151	molecular_function	molybdenum ion binding
C	0030288	cellular_component	outer membrane-bounded periplasmic space
C	0042597	cellular_component	periplasmic space
C	0046872	molecular_function	metal ion binding
C	0047770	molecular_function	carboxylate reductase activity
C	0110095	biological_process	cellular detoxification of aldehyde

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES A 230

Chain	Residue
A	GLN157
A	CYS158
A	GLY159
A	CYS161
A	CYS208
A	ARG209
A	CYS210

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FES A 231

Chain	Residue
A	ASP100
A	GLY102
A	GLN103
A	CYS104
A	GLY105
A	CYS107
A	CYS119
A	GLY98
A	CYS99

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD A 1227

Chain	Residue
C	ARG272

site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 1228

Chain	Residue
A	GLY113

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 1229

Chain	Residue
A	GLN103
A	GOL1232
C	ARG272
C	ASP655

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACT A 1231

Chain	Residue
A	ARG114
B	ASP77

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 1232

Chain	Residue
A	HIS101
A	GLN103
A	CL1229
A	HOH2076
A	HOH2175
B	ASP36
B	TYR123
C	PRO273
C	ASP655

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 1233

Chain	Residue
A	HIS153
A	ASN215
A	HOH2169
C	ARG623
C	CL1737

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 B 320

Chain	Residue
B	CYS119
B	CYS129
B	ASN130
B	LYS131
B	CYS138
B	ALA156
B	CYS157
B	ILE158
B	ALA159

site_id	BC1
Number of Residues	32
Details	BINDING SITE FOR RESIDUE FAD B 321

Chain	Residue
A	GLY102
B	LYS26
B	PHE27
B	ALA29
B	GLY30
B	GLY31
B	THR32
B	ASN33
B	LEU34
B	GLY98
B	ALA99
B	LEU103
B	ALA107
B	THR108
B	ALA110
B	GLY111
B	ASN112
B	LEU114
B	GLN115
B	SER163
B	ASP164
B	LEU212
B	ILE213
B	LYS230
B	ALA238
B	PHE239
B	HOH2017
B	HOH2027
B	HOH2054
B	HOH2063
B	HOH2093
B	HOH2245

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL B 1318

Chain	Residue
B	HOH2080
C	HOH2058
C	HOH2533

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL B 1319

Chain	Residue
B	GLY135
B	LYS199

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL B 1320

Chain	Residue
B	ARG170
B	GLU269

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT B 1321

Chain	Residue
B	THR62
B	ASP63
B	ALA64
B	HOH2047
B	HOH2058

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 1322

Chain	Residue
B	LYS264
B	TRP266
B	ARG267
B	ILE268
B	HOH2148
B	HOH2150
B	IOD3000

site_id	BC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 1323

Chain	Residue
B	ALA238
B	PHE239
B	HOH2246
B	HOH2247
B	HOH2248
C	ALA657
C	GLU660
B	GLN147

site_id	BC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD B 3000

Chain	Residue
B	GOL1322

site_id	BC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CSD C 395

Chain	Residue
C	VAL387
C	THR393
C	ARG394
C	PHE396
C	TYR581
C	GLN582
C	HOH2392
C	HOH2401

site_id	CC1
Number of Residues	33
Details	BINDING SITE FOR RESIDUE MCN C 921

Chain	Residue
A	GLN157
A	CYS210
C	GLY240
C	GLY241
C	PHE242
C	GLY243
C	ARG350
C	ILE468
C	GLY469
C	THR470
C	GLY471
C	SER472
C	GLY507
C	GLY508
C	GLN509
C	TRP510
C	GLY511
C	ALA512
C	ALA613
C	ARG615
C	LEU617
C	ASN618
C	THR621
C	GLN625
C	ALA687
C	LYS688
C	VAL690
C	GLY691
C	GLU692
C	MOS922
C	HOH2463
C	HOH2464
C	HOH2479

site_id	CC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE MOS C 922

Chain	Residue
C	GLN211
C	GLY243
C	LEU246
C	ALA348
C	MET349
C	ARG350
C	PRO352
C	GLY508
C	GLU692
C	MCN921
C	HOH2558

site_id	CC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD C 1732

Chain	Residue
C	ASN47

site_id	CC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL C 1735

Chain	Residue
C	ARG527
C	HOH2016

site_id	CC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL C 1737

Chain	Residue
A	GOL1233

site_id	CC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL C 1738

Chain	Residue
A	ALA53
C	PHE674
C	HOH2068

site_id	CC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT C 1739

Chain	Residue
C	ARG440
C	HOH2437
C	HOH2558

site_id	CC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACT C 1740

Chain	Residue
C	VAL320
C	GLU324

site_id	CC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL C 1741

Chain	Residue
C	GLU641
C	TYR717
C	LYS723

site_id	DC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 1742

Chain	Residue
C	ILE25
C	ASP26
C	TYR237
C	GLN295
C	ALA492
C	VAL493
C	HOH2472

Functional Information from PROSITE/UniProt

site_id	PS00197
Number of Residues	9
Details	2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CDHGQCGAC

Chain	Residue	Details
A	CYS99-CYS107

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	76
Details	Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	38
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27622978","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5G5G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5G5H","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27622978","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5G5H","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	222
Details	Domain: {"description":"FAD-binding PCMH-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00718","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"19368556","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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