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1DMS

STRUCTURE OF DMSO REDUCTASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0009033molecular_functiontrimethylamine-N-oxide reductase activity
A0009055molecular_functionelectron transfer activity
A0009061biological_processanaerobic respiration
A0016491molecular_functionoxidoreductase activity
A0030151molecular_functionmolybdenum ion binding
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0043546molecular_functionmolybdopterin cofactor binding
A0046872molecular_functionmetal ion binding
A0050626molecular_functiontrimethylamine-N-oxide reductase (cytochrome c) activity
Functional Information from PDB Data
site_idAC1
Number of Residues34
DetailsBINDING SITE FOR RESIDUE PGD A 782
ChainResidue
ATYR114
AGLY433
AASN434
AHIS438
AGLN440
AHIS458
AASP459
APHE460
ATHR463
AALA475
AARG481
AGLY115
AASP511
AALA641
AHIS643
AHIS649
ASER650
AGLN651
AGLU715
AASN737
AGLY754
AGLN755
ATRP116
A2MO784
AHOH979
AHOH983
AHOH997
AHOH1014
ALYS117
ASER118
ATYR146
ASER147
AARG326
AGLY432

site_idAC2
Number of Residues33
DetailsBINDING SITE FOR RESIDUE PGD A 783
ChainResidue
ATRP116
ASER147
AALA185
ALYS190
ATHR191
AGLN193
AILE220
AASP221
APRO222
AVAL223
ATHR225
APRO240
AGLN241
AASP243
AGLY321
ATRP322
ASER323
AARG326
AMET327
AHIS359
ASER642
AHIS643
APRO644
APHE645
AARG647
ALEU648
AHIS649
AGLN755
A2MO784
AHOH865
AHOH866
AHOH869
AHOH984

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MM4 A 784
ChainResidue
ATYR114
ATRP116
AASP145
ATYR146
ASER147
APGD782
APGD783

Functional Information from PROSITE/UniProt
site_idPS00490
Number of Residues18
DetailsMOLYBDOPTERIN_PROK_2 Prokaryotic molybdopterin oxidoreductases signature 2. TpTArhADIVLPaTTsyE
ChainResidueDetails
ATHR463-GLU480

site_idPS00932
Number of Residues28
DetailsMOLYBDOPTERIN_PROK_3 Prokaryotic molybdopterin oxidoreductases signature 3. AaarGIaDgDvVrVhNdrGqiltgVkVT
ChainResidueDetails
AALA676-THR703

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING:
ChainResidueDetails
AALA143
AGLY754
AGLU176
AVAL219
AGLY249
ASER270
AGLY351
AILE487
AHIS672
AALA678

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:10835270, ECO:0000269|PubMed:10985771, ECO:0000269|PubMed:11502174, ECO:0000269|PubMed:8890912, ECO:0000269|PubMed:9466935, ECO:0000269|Ref.6
ChainResidueDetails
AASP145
AGLY355
ATHR463
AARG467
ASER510
ASER540
AGLY766

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1tmo
ChainResidueDetails
ASER147

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PDB entries from 2024-09-18

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