Structure of PDB 3hbp Chain A

Receptor sequence
>3hbpA (length=373) Species: 9031 (Gallus gallus) [Search protein sequence]
QDPFAGDPPRHPGLRVNSQKPFNAEPPAELLAERFLTPNELFFTRNHLPV
PAVEPSSYRLRVDGPGGGTLSLSLAELRSRFPKHEVTATLQSAGNRRSEM
SRVRPVKGLPWDIGAISTARWGGARLRDVLLHAGFPEELQGEWHVCFEGL
DADPGGAPYGASIPYGRALSPAADVLLAYEMNGTELPRDHGFPVRVVVPG
VVGARSVKWLRRVAVSPDESPSHWQQNDYKGFSPCVDWDTVDYRTAPAIQ
ELPVQSAVTQPRPGAAVPPGELTVKGYAWSGGGREVVRVDVSLDGGRTWK
VARLMGDKAPPGRAWAWALWELTVPVEAGTELEIVCKAVDSSYNVQPDSV
APIWNLRGVLSTAWHRVRVSVQD
3D structure
PDB3hbp The structures of the C185S and C185A mutants of sulfite oxidase reveal rearrangement of the active site.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R138 S185 D321 Y322
Catalytic site (residue number reindexed from 1) R45 S92 D228 Y229
Enzyme Commision number 1.8.3.1: sulfite oxidase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 MOM A R138 S185 A297 Y322 R45 S92 A204 Y229
BS02 SO3 A R190 Y322 R97 Y229
Gene Ontology
Molecular Function
GO:0008482 sulfite oxidase activity
GO:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0030151 molybdenum ion binding
GO:0043546 molybdopterin cofactor binding
GO:0046872 metal ion binding
Biological Process
GO:0006790 sulfur compound metabolic process
Cellular Component
GO:0005739 mitochondrion
GO:0005758 mitochondrial intermembrane space

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3hbp, PDBe:3hbp, PDBj:3hbp
PDBsum3hbp
PubMed20356030
UniProtP07850|SUOX_CHICK Sulfite oxidase (Gene Name=SUOX)

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