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4FA1

Crystal Structure of WT MauG in Complex with Pre-Methylamine Dehydrogenase Aged 130 Days.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004130molecular_functioncytochrome-c peroxidase activity
A0009055molecular_functionelectron transfer activity
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
B0004130molecular_functioncytochrome-c peroxidase activity
B0009055molecular_functionelectron transfer activity
B0016491molecular_functionoxidoreductase activity
B0020037molecular_functionheme binding
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
B0098869biological_processcellular oxidant detoxification
C0009308biological_processamine metabolic process
C0016491molecular_functionoxidoreductase activity
C0016638molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors
C0030058molecular_functionamine dehydrogenase activity
C0030288cellular_componentouter membrane-bounded periplasmic space
C0042597cellular_componentperiplasmic space
C0052876molecular_functionmethylamine dehydrogenase (amicyanin) activity
D0016491molecular_functionoxidoreductase activity
D0030058molecular_functionamine dehydrogenase activity
D0030416biological_processmethylamine metabolic process
D0042597cellular_componentperiplasmic space
D0052876molecular_functionmethylamine dehydrogenase (amicyanin) activity
E0009308biological_processamine metabolic process
E0016491molecular_functionoxidoreductase activity
E0016638molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors
E0030058molecular_functionamine dehydrogenase activity
E0030288cellular_componentouter membrane-bounded periplasmic space
E0042597cellular_componentperiplasmic space
E0052876molecular_functionmethylamine dehydrogenase (amicyanin) activity
F0016491molecular_functionoxidoreductase activity
F0030058molecular_functionamine dehydrogenase activity
F0030416biological_processmethylamine metabolic process
F0042597cellular_componentperiplasmic space
F0052876molecular_functionmethylamine dehydrogenase (amicyanin) activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AASN66
ATHR275
APRO277
AHOH513
AHOH526
AHOH579
AHOH588

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEC A 402
ChainResidue
ACYS31
ACYS34
AHIS35
ASER54
AARG65
ATHR67
APRO68
ALEU70
AGLN91
APHE92
ATRP93
AARG96
ALEU100
AGLN103
AALA104
APRO107
AGLU113
AMET114
AGLN163
ALYS265
AHOH638
AHOH639
AGLN29
ASER30

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEC A 403
ChainResidue
ATRP93
AASN200
ACYS201
ACYS204
AHIS205
AHIS224
ALEU228
APHE264
APRO267
AMET279
AHIS280
ALEU287
ATYR294
ASER324
AGLU327
AHOH503
AHOH520
AHOH536
AHOH588

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 404
ChainResidue
AASN231
ATHR233
AHOH596
AHOH607

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 401
ChainResidue
BASN66
BTHR275
BPRO277
BHOH515
BHOH519
BHOH538
BHOH574

site_idAC6
Number of Residues28
DetailsBINDING SITE FOR RESIDUE HEC B 402
ChainResidue
BGLN29
BSER30
BCYS31
BCYS34
BHIS35
BSER54
BVAL55
BARG65
BTHR67
BPRO68
BLEU70
BGLN91
BPHE92
BTRP93
BARG96
BLEU100
BGLN103
BALA104
BPRO107
BGLU113
BMET114
BLEU159
BGLN163
BLYS265
BHOH589
BHOH614
BHOH708
BHOH723

site_idAC7
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEC B 403
ChainResidue
BMET279
BHIS280
BLEU287
BTYR294
BSER324
BGLU327
BHOH515
BHOH519
BHOH522
BHOH552
BHOH633
BTRP93
BASN200
BCYS201
BCYS204
BHIS205
BHIS224
BLEU228
BPHE264
BPRO267
BTYR278

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 404
ChainResidue
BLEU250
BARG252
BILE255
BHOH680
BHOH683
BHOH716

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 405
ChainResidue
BALA164
BARG215

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT D 401
ChainResidue
DARG35
DLEU37
DGLU38

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MES F 401
ChainResidue
BALA138
BLEU139
BGLY141
FARG35
FLEU37
FGLU38

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Tryptophylquinone => ECO:0000269|PubMed:1409575
ChainResidueDetails
CTRQ57
ETRQ57
ACYS201
ACYS204
BCYS31
BCYS34
BCYS201
BCYS204

site_idSWS_FT_FI2
Number of Residues4
DetailsCROSSLNK: Tryptophan tryptophylquinone (Trp-Trp) => ECO:0000269|PubMed:1409575
ChainResidueDetails
CTRQ57
CTRP108
ETRQ57
ETRP108
BHIS205
BHIS280

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 13
ChainResidueDetails
CASP32electrostatic stabiliser, proton acceptor, proton donor
CTRQ57proton acceptor, proton donor, proton relay
CASP76electrostatic stabiliser, proton acceptor, proton donor
CTRP108proton acceptor, proton donor, proton relay, single electron donor
CTYR119steric role
CTHR122electrostatic stabiliser

site_idMCSA2
Number of Residues6
DetailsM-CSA 13
ChainResidueDetails
EASP32electrostatic stabiliser, proton acceptor, proton donor
ETRQ57proton acceptor, proton donor, proton relay
EASP76electrostatic stabiliser, proton acceptor, proton donor
ETRP108proton acceptor, proton donor, proton relay, single electron donor
ETYR119steric role
ETHR122electrostatic stabiliser

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PDB entries from 2024-07-17

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