Structure of PDB 4ywo Chain A

Receptor sequence
>4ywoA (length=444) Species: 399549 (Metallosphaera sedula DSM 5348) [Search protein sequence]
SQDPMHKLAIIGYGAAGFAAMIKANELGVKPVLIGKGEIGGTCVNVGCVP
SKRMLYIAEIYKKAREVTGSEVYPPFSSFQEKDGLVQEMRKTKYEDLLSY
YDVELIQGEARFISPHAVKVNGQVIEAEKFVIATGSSPLIPRIPGLDKVG
FWTNREALSPDRRIDSLAVIGGRALALEFAQMYSRMKVEVAILQRSPVLI
PDWEPEASVEARRIMENDGVAVVTGVNVKEVRKGAGKIVITDKGEVEADE
ILLATGRKPNVDLGLENAGVRLNERGGIKVDDELRTDNPHIYAAGDVLGG
KMLEALAGRQGSIATENALTGSHKRVDENAVPQVIFTQPNLARVGLTEAE
ARAKEGEVEARVLPMSSVAKAEIINSRLGFVKMVTMNGRIVGVHAVGENV
AEMIGEAALAIRFGATVHDLIDTVHMFPTIAESLRLVALAFRSD
3D structure
PDB4ywo Biochemical and Structural Properties of a Thermostable Mercuric Ion Reductase from Metallosphaera sedula.
ChainA
Resolution1.62 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A11 I35 C39 C44 S47 A170 E174 G304 H421 F423 E428
Catalytic site (residue number reindexed from 1) A15 I39 C43 C48 S51 A174 E178 G308 H425 F427 E432
Enzyme Commision number 1.16.1.1: mercury(II) reductase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FAD A G8 G10 K32 G37 T38 C39 G43 C44 K48 A106 A129 T130 G131 N150 L171 L259 G291 D292 M298 L299 E300 A303 G12 G14 K36 G41 T42 C43 G47 C48 K52 A110 A133 T134 G135 N154 L175 L263 G295 D296 M302 L303 E304 A307
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016152 mercury (II) reductase (NADP+) activity
GO:0016491 oxidoreductase activity
GO:0016668 oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
GO:0045340 mercury ion binding
GO:0046872 metal ion binding
GO:0050660 flavin adenine dinucleotide binding
GO:0050661 NADP binding
Biological Process
GO:0050787 detoxification of mercury ion

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Molecular Function
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Biological Process
External links
PDB RCSB:4ywo, PDBe:4ywo, PDBj:4ywo
PDBsum4ywo
PubMed26217660
UniProtA4YG49

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