Structure of PDB 7o26 Chain A

Receptor sequence
>7o26A (length=347) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence]
MTGREILEKLERREFTREVLKEALSINDRGFNEALFKLADEIRRKYVGDE
VHIRAIIEFSNVCRKNCLYCGLRRDNKNLKRYRMTPEEIVERARLAVQFG
AKTIVLQSGEDPYYMPDVISDIVKEIKKMGVAVTLSLGEWPREYYEKWKE
AGADRYLLRHETANPVLHRKLRPDTSFENRLNCLLTLKELGYETGAGSMV
GLPGQTIDDLVDDLLFLKEHDFDMVGIGPFIPHPDTPLANEKKGDFTLTL
KMVALTRILLPDSNIPATTAMGTIVPGGREITLRCGANVIMPNWTPSPYR
QLYQLYPGKICVFEKDTACIPCVMKMIELLGRKPGRDWGGRKRVFET
3D structure
PDB7o26 Crystal Structure of the [FeFe]-Hydrogenase Maturase HydE Bound to Complex-B.
ChainA
Resolution1.5 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) 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 CYS A T269 A270 Y306 T269 A270 Y306
BS02 MET A S108 G138 Y303 S108 G138 Y303
BS03 FES A R279 C311 C319 C322 V323 R279 C311 C319 C322 V323
BS04 SF4 A C63 K65 C67 C70 C63 K65 C67 C70
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:7o26, PDBe:7o26, PDBj:7o26
PDBsum7o26
PubMed34048236
UniProtQ9X0Z6|HYDE_THEMA [FeFe] hydrogenase maturase subunit HydE (Gene Name=TM_1269)

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