Structure of PDB 5ff3 Chain A

Receptor sequence

>5ff3A (length=347) Species: 243274 (Thermotoga maritima MSB8)

MTGREILEKLERREFTREVLKEALSINDRGFNEALFKLADEIRRKYVGDE
VHIRAIIEFSNVCRKNCLYCGLRRDNKNLKRYRMTPEEIVERARLAVQFG
AKTIVLQSGEDPYYMPDVISDIVKEIKKMGVAVTLSLGEWPREYYEKWKE
AGADRYLLRHETANPVLHRKLRPDTSFENRLNCLLTLKELGYETGAGSMV
GLPGQTIDDLVDDLLFLKEHDFDMVGIGPFIPHPDTPLANEKKGDFTLTL
KMVALTRILLPDSNIPATTAMGTIVPGGREITLRCGANVIMPNWTPSPYR
QLYQLYPGKICVFEKDTACIPCVMKMIELLGRKPGRDWGGRKRVFET

3D structure

• PDB: 5ff3 Carbon-sulfur bond-forming reaction catalysed by the radical SAM enzyme HydE.
• Chain: A
• Resolution: 1.18 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C63 C67 C70 V105 T134 G195 P266
• Catalytic site (residue number reindexed from 1): C63 C67 C70 V105 T134 G195 P266
• 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	SF4	A	C63 K65 C67 C70	C63 K65 C67 C70
BS02	FES	A	R279 C311 C319 C322	R279 C311 C319 C322
BS03	SAH	A	Y69 Q107 S108 R159 E161 M199 I231 L305 Y306	Y69 Q107 S108 R159 E161 M199 I231 L305 Y306
BS04	PRS	A	R159 T269 A270 Y306	R159 T269 A270 Y306

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

External links

• PDB: RCSB:5ff3, PDBe:5ff3, PDBj:5ff3
• PDBsum: 5ff3
• PubMed: 27102684
• UniProt: Q9X0Z6|HYDE_THEMA [FeFe] hydrogenase maturase subunit HydE (Gene Name=TM_1269)