Structure of PDB 5ve5 Chain A

Receptor sequence
>5ve5A (length=350) Species: 398527 (Paraburkholderia phytofirmans PsJN) [Search protein sequence]
SHMLIFRQLFDQQSSTYTYLLADSTTREAVLIDPVFEQVRRDAALIEELG
LHLLYTIDTHVHADHVTGAWMLNRRIGSRIAISAASGAEGADRYLSHGDK
VEFGTRYLTVRATPGHTDGCITLVLDNETMAFTGDCLLIRGTGRTDFQRG
DAHTMFRAVHGQIFTLPTACLLYPAHDYRGLTVTSVGEERRFNPRLGGEL
CEEDFTGYMTNLHLPHPKQIDVAVPANLKCGLAEPDWAPLTCSFAGIWEI
NAQWLEENLRAVEIVDVREPEEFNGPLGRIPAARLISLGELAGRTAELTK
DRPIVTVSRAGGRSAQATVMLRQAGFERVANLPGGMLRWRAEGRVVENGS
3D structure
PDB5ve5 Structural and biochemical analyses indicate that a bacterial persulfide dioxygenase-rhodanese fusion protein functions in sulfur assimilation.
ChainA
Resolution2.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R25 H58 H60 D62 H63 H114 D133 H174
Catalytic site (residue number reindexed from 1) R27 H60 H62 D64 H65 H116 D135 H176
Enzyme Commision number '1.13.11.18
2.8.1.1'
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 FE A H58 H114 D133 H60 H116 D135
BS02 GSH A H114 D133 G141 R142 Y176 L212 P215 K216 H116 D135 G143 R144 Y178 L214 P217 K218
Gene Ontology
Molecular Function
GO:0046872 metal ion binding
GO:0050313 sulfur dioxygenase activity
Biological Process
GO:0006749 glutathione metabolic process
GO:0070813 hydrogen sulfide metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5ve5, PDBe:5ve5, PDBj:5ve5
PDBsum5ve5
PubMed28684420
UniProtB2TEQ2

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