Structure of PDB 4htr Chain A

Receptor sequence
>4htrA (length=441) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
RCRLPGGVITTKQWQAIDKFAGENTIYGSIRLTNRQTFQFHGILPVHQML
HSVGLDAMNRNVLCTSNPYESQLHAEAYEWAKKISEHLLPKFKTTVVIPP
QNDIDLHANDMNFVAIAENGKLVGFNLLVGGGLSIEHGNKKTYARTASEF
GYLPLEHTLAVAEAVVTTQRDWGNNAKTKYTLERVGVETFKAEVERRAGI
KFEPIRPYEFTGRGDRIGWVKGIDDNWHLTLFIENGRILDYPARPLKTGL
LEIAKIHKGDFRITANQNLIIAGVPESEKAKIEKIAKESGLMNAVTPQRE
NSMACVSFPTCPLAMAEAERFLPSFIDNIDNLMAKHGVSDEHIVMRVTGC
PNGCGRAMLAEVGLVGKAPGRYNLHLGGNRIGTRIPRMYKENITEPEILA
SLDELIGRWAKEREAGEGFGDFTVRAGIIRPVLDPARDLWD
3D structure
PDB4htr Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer.
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R83 R153 K215 K217 A394 C434 C440 C479 C483
Catalytic site (residue number reindexed from 1) R1 R60 K91 K93 A265 C305 C311 C350 C354
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:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0050661 NADP binding
GO:0051536 iron-sulfur cluster binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0008652 amino acid 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:4htr, PDBe:4htr, PDBj:4htr
PDBsum4htr
PubMed23153334
UniProtP17846|CYSI_ECOLI Sulfite reductase [NADPH] hemoprotein beta-component (Gene Name=cysI)

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