Structure of PDB 7o1t Chain A

Receptor sequence
>7o1tA (length=356) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MWSHPQFEKASTGREILEKLERREFTREVLKEALSINDRGFNEALFKLAD
EIRRKYVGDEVHIRAIIEFSNVCRKNCLYCGLRRDNKNLKRYRMTPEEIV
ERARLAVQFGAKTIVLQSGEDPYYMPDVISDIVKEIKKMGVAVTLSLGEW
PREYYEKWKEAGADRYLLRHETANPVLHRKLRPDTSFENRLNCLLTLKEL
GYETGAGSMVGLPGQTIDDLVDDLLFLKEHDFDMVGIGPFIPHPDTPLAN
EKKGDFTLTLKMVALTRILLPDSNIPATTAMGTIVPGGREITLRCGANVI
MPNWTPSPYRQLYQLYPGKISVFEKDTASIPSVMKMIELLGRKPGRDWGG
RKRVFE
3D structure
PDB7o1t 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) C73 C77 C80 V115 T144 G205 P276
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 T279 A280 Y316
BS02 5X8 A Y69 C70 Q107 S108 R159 E161 R180 M199 I231 Y306 Y79 C80 Q117 S118 R169 E171 R190 M209 I241 Y316
BS03 SF4 A C63 K65 C67 C70 C73 K75 C77 C80
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:7o1t, PDBe:7o1t, PDBj:7o1t
PDBsum7o1t
PubMed34048236
UniProtQ9X0Z6|HYDE_THEMA [FeFe] hydrogenase maturase subunit HydE (Gene Name=TM_1269)

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