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4FB1

Crystal Structure of WT MauG in Complex with Pre-Methylamine Dehydrogenase Aged 60 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
AHOH514
AHOH523
AHOH545
AHOH572

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEC A 402
ChainResidue
ACYS31
ACYS34
AHIS35
ASER54
AVAL55
AARG65
ATHR67
APRO68
ALEU70
AGLN91
APHE92
ATRP93
AARG96
ALEU100
AGLN103
AALA104
APRO107
AGLU113
AMET114
AGLN163
ALYS265
AGLN29
ASER30

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEC A 403
ChainResidue
ATRP93
AASN200
ACYS201
ACYS204
AHIS205
AHIS224
ALEU228
APHE264
APRO267
AVAL272
ATYR278
AMET279
AHIS280
ALEU287
ATYR294
AGLU327
ALEU334
AHOH520
AHOH540
AHOH545
AHOH565

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 404
ChainResidue
ALEU250
AARG252
AILE255

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 401
ChainResidue
BASN66
BTHR275
BPRO277
BHOH508
BHOH510
BHOH521
BHOH598

site_idAC6
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEC B 402
ChainResidue
BGLN29
BSER30
BCYS31
BCYS34
BHIS35
BSER54
BARG65
BTHR67
BPRO68
BLEU70
BGLN91
BPHE92
BTRP93
BARG96
BLEU100
BGLN103
BALA104
BPRO107
BGLU113
BMET114
BGLN163
BLYS265
BHOH618
BHOH636
BHOH640

site_idAC7
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEC B 403
ChainResidue
BHIS280
BLEU287
BTYR294
BSER324
BGLU327
BLEU334
BHOH508
BHOH510
BHOH514
BHOH562
BHOH566
BTRP93
BASN200
BCYS201
BCYS204
BHIS205
BHIS224
BILE226
BLEU228
BPHE264
BVAL266
BPRO267
BTYR278
BMET279

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA B 404
ChainResidue
BLEU250
BARG252
BILE255

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA B 405
ChainResidue
BASN231
BTHR233
BHOH609

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MES D 401
ChainResidue
AALA138
AGLY141
DARG35
DLEU37
DGLU38

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MES F 401
ChainResidue
BLEU139
BPHE140
FARG35
FLEU37
FGLU38

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Tryptophylquinone => ECO:0000269|PubMed:1409575
ChainResidueDetails
C0AF57
E0AF57
ACYS201
ACYS204
BCYS31
BCYS34
BCYS201
BCYS204

site_idSWS_FT_FI2
Number of Residues4
DetailsCROSSLNK: Tryptophan tryptophylquinone (Trp-Trp) => ECO:0000269|PubMed:1409575
ChainResidueDetails
C0AF57
CTRP108
E0AF57
ETRP108
BHIS205
BHIS280

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 13
ChainResidueDetails
CASP32electrostatic stabiliser, proton acceptor, proton donor
C0AF57proton 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
E0AF57proton 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 2024-08-07

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