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5G5H

Escherichia coli Periplasmic Aldehyde Oxidase R440H mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
B0005515molecular_functionprotein binding
B0009056biological_processcatabolic process
B0016491molecular_functionoxidoreductase activity
B0016903molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
B0047770molecular_functioncarboxylate reductase activity
B0050660molecular_functionflavin adenine dinucleotide binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
B0071949molecular_functionFAD binding
B0110095biological_processcellular detoxification of aldehyde
B1990204cellular_componentoxidoreductase complex
C0005506molecular_functioniron ion binding
C0005515molecular_functionprotein binding
C0006974biological_processDNA damage response
C0009056biological_processcatabolic process
C0016491molecular_functionoxidoreductase activity
C0016903molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors
C0030151molecular_functionmolybdenum ion binding
C0030288cellular_componentouter membrane-bounded periplasmic space
C0042597cellular_componentperiplasmic space
C0046872molecular_functionmetal ion binding
C0047770molecular_functioncarboxylate reductase activity
C0110095biological_processcellular detoxification of aldehyde
C1990204cellular_componentoxidoreductase complex
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FES A 1226
ChainResidue
AGLN157
ACYS158
AGLY159
ACYS161
ACYS208
AARG209
ACYS210

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FES A 1227
ChainResidue
AASP100
AGLY102
AGLN103
ACYS104
AGLY105
ACYS107
ACYS119
AGLY98
ACYS99

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD A 1228
ChainResidue
CARG272
CACT1743

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 1229
ChainResidue
AVAL184
AVAL186
AGLU193
ATHR195
AGLU198

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SF4 B 1317
ChainResidue
BCYS119
BCYS129
BCYS138
BALA156
BCYS157
BILE158

site_idAC6
Number of Residues32
DetailsBINDING SITE FOR RESIDUE FAD B 1318
ChainResidue
AGLY102
BLYS26
BPHE27
BALA29
BGLY30
BGLY31
BTHR32
BASN33
BLEU34
BGLY98
BALA99
BLEU103
BALA107
BTHR108
BALA110
BGLY111
BASN112
BLEU114
BGLN115
BPRO162
BSER163
BASP164
BLEU212
BILE213
BLYS230
BTYR237
BALA238
BPHE239
BHOH2040
BHOH2058
BHOH2062
BHOH2155

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 1319
ChainResidue
BGLN249

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD B 1320
ChainResidue
BGLN147
BTHR160

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 1321
ChainResidue
BGLN147

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 1322
ChainResidue
BASN130
BGLY135
BLYS199

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 1324
ChainResidue
BHOH2154

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CSD C 395
ChainResidue
CVAL387
CTHR393
CARG394
CPHE396
CSER397
CTYR581
CGLN582

site_idBC4
Number of Residues34
DetailsBINDING SITE FOR RESIDUE MCN C 1732
ChainResidue
CALA622
CGLN625
CLYS688
CGLY689
CVAL690
CGLY691
CGLU692
CMOS1733
CHOH2324
CHOH2325
CHOH2339
AGLN157
ACYS210
CGLY240
CGLY241
CPHE242
CGLY243
CARG350
CILE468
CGLY469
CTHR470
CGLY471
CSER472
CGLY507
CGLY508
CGLN509
CTRP510
CGLY511
CALA512
CARG615
CILE616
CLEU617
CASN618
CTHR621

site_idBC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MOS C 1733
ChainResidue
CGLN211
CGLY243
CMET349
CARG350
CPRO352
CGLY508
CGLU692
CMCN1732
CHOH2338

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IOD C 1734
ChainResidue
AGLN103
CARG272
CASP655

site_idBC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD C 1735
ChainResidue
CASN47

site_idBC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL C 1738
ChainResidue
CARG406

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL C 1739
ChainResidue
CARG527
CGLN542

site_idCC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL C 1740
ChainResidue
AHOH2021

site_idCC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT C 1742
ChainResidue
CASP93
CLYS94
CTRP215
CASP219

site_idCC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACT C 1743
ChainResidue
ALYS97
AASP100
AIOD1228
AHOH2041
CPHE120
CMET269
CPRO271
CHOH2050

site_idCC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL C 1744
ChainResidue
CTRP41
CTHR170
CSER171
CASP497
CHOH2047

site_idCC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL C 1745
ChainResidue
CTHR315
CPRO316
CGLU317
CTHR318
CALA348
CPRO352

site_idCC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL C 1746
ChainResidue
CLEU29
CTYR237
CGLN295
CTYR473
CVAL493

Functional Information from PROSITE/UniProt
site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CDHGQCGAC
ChainResidueDetails
ACYS99-CYS107

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:19368556
ChainResidueDetails
CGLU692
BTHR108
BCYS119
BCYS129
BCYS138
BCYS157
BASP164
BILE213
BLYS230

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:27622978, ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H
ChainResidueDetails
CGLY241
CILE468
CGLY511
CARG615
CGLN625
CLYS688

225946

PDB entries from 2024-10-09

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