Structure of PDB 6gep Chain A

Receptor sequence
>6gepA (length=456) Species: 37762 (Escherichia coli B) [Search protein sequence]
LLRCRLPGGVITTKQWQAIDKFAGENTIYGSIRLTNRQTFQFHGILPVHQ
MLHSVGLDALNDMNRNVLCTSNPYESQLHAEAYEWAKKISEHLLPTYLPR
KFKTTVVIPPQNDIDLHANDMNFVAIAENGKLVGFNLLVGGGLSIEHGNK
KTYARTASEFGYLPLEHTLAVAEAVVTTQRDWGNRTDRKNAKTKYTLERV
GVETFKAEVERRAGIKFEPIRPYEFTGRGDRIGWVKGIDDNWHLTLFIEN
GRILDYPARPLKTGLLEIAKIHKGDFRITANQNLIIAGVPESEKAKIEKI
AKESGLMNAVTPQRENSMACVSFPTCPLAMAEAERFLPSFIDNIDNLMAK
HGVSDEHIVMRVTGCPNGCGRAMLAEVGLVGKAPGRYNLHLGGNRIGTRI
PRMYKENITEPEILASLDELIGRWAKEREAGEGFGDFTVRAGIIRPVLDP
ARDLWD
3D structure
PDB6gep Probing the catalytic mechanism of sulfite reductase by X-ray crystallography: structures of the Escherichia coli hemoprotein in complex with substrates, inhibitors, intermediates, and products.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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)

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:6gep, PDBe:6gep, PDBj:6gep
PDBsum6gep
PubMed9315849
UniProtP17846|CYSI_ECOLI Sulfite reductase [NADPH] hemoprotein beta-component (Gene Name=cysI)

[Back to BioLiP]