Structure of PDB 3aop Chain A

Receptor sequence
>3aopA (length=453) Species: 37762 (Escherichia coli B) [Search protein sequence]
LRCRLPGGVITTKQWQAIDKFAGENTIYGSIRLTNRQTFQFHGILPVHQM
LHSVGLDALNDMNRNVLCTSNPYESQLHAEAYEWAKKISEHLLPLPRKFK
TTVVIPPQNDIDLHANDMNFVAIAENGKLVGFNLLVGGGLSIEHGNKKTY
ARTASEFGYLPLEHTLAVAEAVVTTQRDWGNRTDRKNAKTKYTLERVGVE
TFKAEVERRAGIKFEPIRPYEFTGRGDRIGWVKGIDDNWHLTLFIENGRI
LDYPARPLKTGLLEIAKIHKGDFRITANQNLIIAGVPESEKAKIEKIAKE
SGLMNAVTPQRENSMACVSFPTCPLAMAEAERFLPSFIDNIDNLMAKHGV
SDEHIVMRVTGCPNGCGRAMLAEVGLVGKAPGRYNLHLGGNRIGTRIPRM
YKENITEPEILASLDELIGRWAKEREAGEGFGDFTVRAGIIRPVLDPARD
LWD
3D structure
PDB3aop Structures of the siroheme- and Fe4S4-containing active center of sulfite reductase in different states of oxidation: heme activation via reduction-gated exogenous ligand exchange.
ChainA
Resolution2.1 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) R2 R64 K98 K100 A277 C317 C323 C362 C366
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:3aop, PDBe:3aop, PDBj:3aop
PDBsum3aop
PubMed9315848
UniProtP17846|CYSI_ECOLI Sulfite reductase [NADPH] hemoprotein beta-component (Gene Name=cysI)

[Back to BioLiP]