Structure of PDB 6c3m Chain A

Receptor sequence
>6c3mA (length=465) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MLLRCRLPGGVITTKQWQAIDKFAGENTIYGSIRLTNRQTFQFHGILKKN
VKPVHQMLHSVGLDALATANDMNRNVLCTSNPYESQLHAEAYEWAKKISE
HLLPTYLPRKFKTTVVIPPQNDIDLHANDMNFVAIAENGKLVGFNLLVGG
GLSIEHGNKKTYARTASEFGYLPLEHTLAVAEAVVTTQRDWGNRTDRKNA
KTKYTLERVGVETFKAEVERRAGIKFEPIRPYEFTGRGDRIGWVKGIDDN
WHLTLFIENGRILDYPARPLKTGLLEIAKIHKGDFRITANQNLIIAGVPE
SEKAKIEKIAKESGLMNAVTPQRENSMACVSFPTCPLAMAEAERFLPSFI
DNIDNLMAKHGVSDEHIVMRVTGCPNGCGRAMLAEVGLVGKAPGRYNLHL
GGNRIGTRIPRMYKENITEPEILASLDELIGRWAKEREAGEGFGDFTVRA
GIIRPVLDPARDLWD
3D structure
PDB6c3m The role of extended Fe4S4cluster ligands in mediating sulfite reductase hemoprotein activity.
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) A394
Catalytic site (residue number reindexed from 1) A289
Enzyme Commision number 1.8.1.2: assimilatory sulfite reductase (NADPH).
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004783 sulfite reductase (NADPH) activity
GO:0016002 sulfite reductase activity
GO:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0050311 sulfite reductase (ferredoxin) activity
GO:0050661 NADP binding
GO:0051536 iron-sulfur cluster binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0000103 sulfate assimilation
GO:0008652 amino acid biosynthetic process
GO:0019344 cysteine biosynthetic process
GO:0070814 hydrogen sulfide biosynthetic process
Cellular Component
GO:0009337 sulfite reductase complex (NADPH)

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6c3m, PDBe:6c3m, PDBj:6c3m
PDBsum6c3m
PubMed29852252
UniProtP17846|CYSI_ECOLI Sulfite reductase [NADPH] hemoprotein beta-component (Gene Name=cysI)

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