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3RN1

Crystal Structure of the W199E-MauG/pre-Methylamine Dehydrogenase Complex

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
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
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 400
ChainResidue
AASN66
ATHR275
APRO277
AHOH377
AHOH378
AHOH385
AHOH394

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 401
ChainResidue
AHOH380
AHOH488
AHOH844
AHOH918
AASN231
ATHR233

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 402
ChainResidue
ALEU250
AARG252
AILE255
AHOH768
AHOH931

site_idAC4
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEC A 500
ChainResidue
AGLN29
ASER30
ACYS31
ACYS34
AHIS35
AVAL55
AARG65
ATHR67
APRO68
ALEU70
AGLN91
APHE92
ATRP93
AARG96
ALEU100
AGLN103
AALA104
APRO107
AGLN163
ALYS265
AHOH441
AHOH526
AHOH1170
AHOH1290

site_idAC5
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEC A 600
ChainResidue
ATRP93
AASN200
ACYS201
ACYS204
AHIS205
AHIS224
ALEU228
APHE264
APRO267
ALEU269
ATYR278
AMET279
AHIS280
ALEU287
ATYR294
ASER324
AGLU327
AHOH378
AHOH385
AHOH423
AHOH439
AHOH452

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 400
ChainResidue
BASN66
BTHR275
BPRO277
BHOH385
BHOH403
BHOH417
BHOH439

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 401
ChainResidue
BASN231
BTHR233
BHOH413
BHOH981
BHOH1088
BHOH1123

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 402
ChainResidue
BLEU250
BARG252
BILE255
BHOH513
BHOH809
BHOH1229

site_idAC9
Number of Residues26
DetailsBINDING SITE FOR RESIDUE HEC B 500
ChainResidue
BGLN103
BALA104
BPRO107
BMET114
BGLN163
BLYS265
BHOH452
BHOH545
BHOH761
BHOH886
BGLN29
BSER30
BCYS31
BCYS34
BHIS35
BSER54
BVAL55
BARG65
BTHR67
BPRO68
BLEU70
BGLN91
BPHE92
BTRP93
BARG96
BLEU100

site_idBC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEC B 600
ChainResidue
BTRP93
BASN200
BCYS201
BCYS204
BHIS205
BHIS224
BLEU228
BPHE264
BPRO267
BTYR278
BMET279
BHIS280
BLEU287
BTYR294
BSER324
BGLU327
BHOH376
BHOH403
BHOH417
BHOH425
BHOH430

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 1PE F 387
ChainResidue
AASN26
AALA121
AARG125
AASP128
FVAL219
FPHE261
FLEU262
FHOH888

site_idBC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PG4 F 388
ChainResidue
DLEU291
FTHR187
FGLN235
FLYS236
FGLY238
FSER255
FSER256
FHOH841
FHOH972
FHOH1039

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT F 389
ChainResidue
FARG35
FLEU37
FGLU38
FHOH498

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 374
ChainResidue
BALA164
BARG215

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: covalent => ECO:0000255|PROSITE-ProRule:PRU00433
ChainResidueDetails
ACYS31
ACYS34
ACYS201
ACYS204
BCYS31
BCYS34
BCYS201
BCYS204

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00433
ChainResidueDetails
AHIS35
AHIS205
AHIS280
BHIS35
BHIS205
BHIS280

222036

PDB entries from 2024-07-03

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