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4YWO

Mercuric reductase from Metallosphaera sedula

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
A0016152molecular_functionmercury (II) reductase (NADP+) activity
A0016491molecular_functionoxidoreductase activity
A0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A0045340molecular_functionmercury ion binding
A0046689biological_processresponse to mercury ion
A0046872molecular_functionmetal ion binding
A0050660molecular_functionflavin adenine dinucleotide binding
A0050661molecular_functionNADP binding
A0050787biological_processdetoxification of mercury ion
Functional Information from PDB Data
site_idAC1
Number of Residues41
Detailsbinding site for residue FAD A 501
ChainResidue
AGLY8
ACYS39
AVAL42
AGLY43
ACYS44
ASER47
ALYS48
AGLY104
AALA106
AALA129
ATHR130
ATYR9
AGLY131
AASN150
AARG253
ALEU259
AGLY291
AASP292
AMET298
ALEU299
AGLU300
AALA303
AGLY10
APHE332
AMET422
APHE423
AHOH601
AHOH605
AHOH609
AHOH623
AHOH636
AHOH652
AHOH684
AALA11
AHOH695
AHOH707
AALA12
AGLY31
ALYS32
AGLY37
ATHR38

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 502
ChainResidue
AILE109
AGLU202
AGLU206
APHE376
AHOH604
AHOH655

site_idAC3
Number of Residues10
Detailsbinding site for residue GOL A 503
ChainResidue
ALEU51
ATYR52
APHE332
ATHR333
AASN336
AASN395
AHOH610
AHOH683
AHOH731
AHOH739

site_idAC4
Number of Residues8
Detailsbinding site for residue GOL A 504
ChainResidue
ATYR52
ALYS59
AGLN334
AILE370
AGLU394
AHOH630
AHOH694
AHOH703

site_idAC5
Number of Residues6
Detailsbinding site for residue GOL A 505
ChainResidue
APHE72
AARG158
AARG159
AILE160
AHOH629
AHOH719

site_idAC6
Number of Residues6
Detailsbinding site for residue GOL A 506
ChainResidue
ALEU280
ALEU294
AGLN306
AVAL322
AGLU324
AHOH686

Functional Information from PROSITE/UniProt
site_idPS00076
Number of Residues11
DetailsPYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnvGCVP
ChainResidueDetails
AGLY36-PRO46

247536

PDB entries from 2026-01-14

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