Structure of PDB 5ff0 Chain A

Receptor sequence
>5ff0A (length=346) Species: 2336 (Thermotoga maritima) [Search protein sequence]
TGREILEKLERREFTREVLKEALSINDRGFNEALFKLADEIRRKYVGDEV
HIRAIIEFSNVCRKNCLYCGLRRDNKNLKRYRMTPEEIVERARLAVQFGA
KTIVLQSGEDPYYMPDVISDIVKEIKKMGVAVTLSLGEWPREYYEKWKEA
GADRYLLRHETANPVLHRKLRPDTSFENRLNCLLTLKELGYETGAGSMVG
LPGQTIDDLVDDLLFLKEHDFDMVGIGPFIPHPDTPLANEKKGDFTLTLK
MVALTRILLPDSNIPATTAMGTIVPGGREITLRCGANVIMPNWTPSPYRQ
LYQLYPGKISVFEKDTASIPSVMKMIELLGRKPGRDWGGRKRVFET
3D structure
PDB5ff0 Carbon-sulfur bond-forming reaction catalysed by the radical SAM enzyme HydE.
ChainA
Resolution1.49 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C63 C67 C70 V105 T134 G195 P266
Catalytic site (residue number reindexed from 1) C62 C66 C69 V104 T133 G194 P265
Enzyme Commision number 1.8.-.-
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 SFS A C63 K65 C67 C70 L72 R73 C62 K64 C66 C69 L71 R72
BS02 MET A Q107 S108 S136 G138 R180 Y303 Q106 S107 S135 G137 R179 Y302
BS03 5X8 A Y69 R159 E161 M199 I231 T269 A270 L305 Y306 Y68 R158 E160 M198 I230 T268 A269 L304 Y305
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016491 oxidoreductase activity
GO:0016740 transferase activity
GO:0046872 metal ion binding
GO:0051536 iron-sulfur cluster binding
GO:0051537 2 iron, 2 sulfur cluster binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0042364 water-soluble vitamin biosynthetic process
GO:0044272 sulfur compound biosynthetic process

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Molecular Function

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Biological Process
External links
PDB RCSB:5ff0, PDBe:5ff0, PDBj:5ff0
PDBsum5ff0
PubMed27102684
UniProtQ9X0Z6|HYDE_THEMA [FeFe] hydrogenase maturase subunit HydE (Gene Name=TM_1269)

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