Structure of PDB 1aop Chain A

Receptor sequence
>1aopA (length=456) Species: 37762 (Escherichia coli B) [Search protein sequence]
LLRCRLPGGVITTKQWQAIDKFAGENTIYGSIRLTNRQTFQFHGILPVHQ
MLHSVGLDALNDMNRNVLCTSNPYESQLHAEAYEWAKKISEHLLPTYLPR
KFKTTVVIPPQNDIDLHANDMNFVAIAENGKLVGFNLLVGGGLSIEHGNK
KTYARTASEFGYLPLEHTLAVAEAVVTTQRDWGNRTDRKNAKTKYTLERV
GVETFKAEVERRAGIKFEPIRPYEFTGRGDRIGWVKGIDDNWHLTLFIEN
GRILDYPARPLKTGLLEIAKIHKGDFRITANQNLIIAGVPESEKAKIEKI
AKESGLMNAVTPQRENSMACVSFPTCPLAMAEAERFLPSFIDNIDNLMAK
HGVSDEHIVMRVTGCPNGCGRAMLAEVGLVGKAPGRYNLHLGGNRIGTRI
PRMYKENITEPEILASLDELIGRWAKEREAGEGFGDFTVRAGIIRPVLDP
ARDLWD
3D structure
PDB1aop Sulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions.
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) R3 R65 K101 K103 A280 C320 C326 C365 C369
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:1aop, PDBe:1aop, PDBj:1aop
PDBsum1aop
PubMed7569952
UniProtP17846|CYSI_ECOLI Sulfite reductase [NADPH] hemoprotein beta-component (Gene Name=cysI)

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