Structure of PDB 5k3x Chain A

Receptor sequence
>5k3xA (length=343) Species: 266834 (Sinorhizobium meliloti 1021) [Search protein sequence]
LETKRSEFGTSIITPEEKLYIKNNVNTPPESILADRDGWKVEISGVKEPR
TLTVAELKTLGLVTAATVLQCSGNGRKYFKDQLTGDQKMSGTPWTVGAAG
CVIWSGVPLKAVVDALGGPAEGARFITGTGGEELPAGLDPKLLVVERSVP
ISNLDNVILAWEMNGRPLSLAHGGPLRMVVPGYSGVNNIKYVKAVAMTEV
ETDAKIQKTSYRVHALGEKGSPDQPSVWEQPVKSWITTPHEAAKAGQVQI
AGVAFGGMNACKSVEVSVDGGQTWQEAEFIGPDLGRFAWRVFALSADLAR
GTYTLVSRATDTEGNVQPEETEMNGAGYGHNGWRAPAVKLTVA
3D structure
PDB5k3x The central active site arginine in sulfite oxidizing enzymes alters kinetic properties by controlling electron transfer and redox interactions.
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) K78 C127 S266 Y267
Catalytic site (residue number reindexed from 1) K22 C71 S210 Y211
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 MSS A Y76 I77 K78 N79 N80 L125 C127 S128 E188 V201 H228 R233 G241 V242 N244 K246 Y247 Y20 I21 K22 N23 N24 L69 C71 S72 E132 V145 H172 R177 G185 V186 N188 K190 Y191
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

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Molecular Function
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Biological Process
External links
PDB RCSB:5k3x, PDBe:5k3x, PDBj:5k3x
PDBsum5k3x
PubMed28986298
UniProtQ92M24

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