Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5G5H

Escherichia coli Periplasmic Aldehyde Oxidase R440H mutant

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
C	1990204	cellular_component	oxidoreductase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES A 1226

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 1227

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	2
Details	BINDING SITE FOR RESIDUE IOD A 1228

Chain	Residue
C	ARG272
C	ACT1743

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT A 1229

Chain	Residue
A	VAL184
A	VAL186
A	GLU193
A	THR195
A	GLU198

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SF4 B 1317

Chain	Residue
B	CYS119
B	CYS129
B	CYS138
B	ALA156
B	CYS157
B	ILE158

site_id	AC6
Number of Residues	32
Details	BINDING SITE FOR RESIDUE FAD B 1318

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	PRO162
B	SER163
B	ASP164
B	LEU212
B	ILE213
B	LYS230
B	TYR237
B	ALA238
B	PHE239
B	HOH2040
B	HOH2058
B	HOH2062
B	HOH2155

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD B 1319

Chain	Residue
B	GLN249

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD B 1320

Chain	Residue
B	GLN147
B	THR160

site_id	AC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL B 1321

Chain	Residue
B	GLN147

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL B 1322

Chain	Residue
B	ASN130
B	GLY135
B	LYS199

site_id	BC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL B 1324

Chain	Residue
B	HOH2154

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CSD C 395

Chain	Residue
C	VAL387
C	THR393
C	ARG394
C	PHE396
C	SER397
C	TYR581
C	GLN582

site_id	BC4
Number of Residues	34
Details	BINDING SITE FOR RESIDUE MCN C 1732

Chain	Residue
C	ALA622
C	GLN625
C	LYS688
C	GLY689
C	VAL690
C	GLY691
C	GLU692
C	MOS1733
C	HOH2324
C	HOH2325
C	HOH2339
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	ARG615
C	ILE616
C	LEU617
C	ASN618
C	THR621

site_id	BC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MOS C 1733

Chain	Residue
C	GLN211
C	GLY243
C	MET349
C	ARG350
C	PRO352
C	GLY508
C	GLU692
C	MCN1732
C	HOH2338

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IOD C 1734

Chain	Residue
A	GLN103
C	ARG272
C	ASP655

site_id	BC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD C 1735

Chain	Residue
C	ASN47

site_id	BC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL C 1738

Chain	Residue
C	ARG406

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL C 1739

Chain	Residue
C	ARG527
C	GLN542

site_id	CC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL C 1740

Chain	Residue
A	HOH2021

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT C 1742

Chain	Residue
C	ASP93
C	LYS94
C	TRP215
C	ASP219

site_id	CC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ACT C 1743

Chain	Residue
A	LYS97
A	ASP100
A	IOD1228
A	HOH2041
C	PHE120
C	MET269
C	PRO271
C	HOH2050

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 1744

Chain	Residue
C	TRP41
C	THR170
C	SER171
C	ASP497
C	HOH2047

site_id	CC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 1745

Chain	Residue
C	THR315
C	PRO316
C	GLU317
C	THR318
C	ALA348
C	PRO352

site_id	CC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 1746

Chain	Residue
C	LEU29
C	TYR237
C	GLN295
C	TYR473
C	VAL493

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)