Structure of PDB 3iiz Chain A

Receptor sequence
>3iizA (length=346) Species: 2336 (Thermotoga maritima) [Search protein sequence]
TGREILEKLERREFTREVLKEALSINDRGFNEALFKLADEIRRKYVGDEV
HIRAIIEFSNVCRKNCLYCGLRRDNKNLKRYRMTPEEIVERARLAVQFGA
KTIVLQSGEDPYYMPDVISDIVKEIKKMGVAVTLSLGEWPREYYEKWKEA
GADRYLLRHETANPVLHRKLRPDTSFENRLNCLLTLKELGYETGAGSMVG
LPGQTIDDLVDDLLFLKEHDFDMVGIGPFIPHPDTPLANEKKGDFTLTLK
MVALTRILLPDSNIPATTAMGTIVPGGREITLRCGANVIMPNWTPSPYRQ
LYQLYPGKICVFEKDTACIPCVMKMIELLGRKPGRDWGGRKRVFET
3D structure
PDB3iiz Unexpected electron transfer mechanism upon AdoMet cleavage in radical SAM proteins
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) 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 SF4 A C63 K65 C67 C70 C62 K64 C66 C69
BS02 SAM A Y69 Q107 S108 G138 R159 E161 M199 I231 L305 Y306 Y68 Q106 S107 G137 R158 E160 M198 I230 L304 Y305
BS03 FES A R279 C311 C319 R278 C310 C318
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:3iiz, PDBe:3iiz, PDBj:3iiz
PDBsum3iiz
PubMed19706452
UniProtQ9X0Z6|HYDE_THEMA [FeFe] hydrogenase maturase subunit HydE (Gene Name=TM_1269)

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