Structure of PDB 4kpo Chain A

Receptor sequence
>4kpoA (length=317) Species: 4577 (Zea mays) [Search protein sequence]
PNSKIIIDTDPGIDDSVAILMAFQMPGVQVLGLTTIFGNCTTEHATRNAL
ILCEKASHLEVPVAEGSHEPLKGGKPHVADFVHGPDGLGNVDLPDPTIKK
VEESATDFLVDKVSRFPGEVSVLALGPLTNIALAIKKDPSFVKNVKKIVV
LGGAFFAAGNATPSAEANIHSDPEAADMVFTSGADIYVVGLNITTQVSFT
DKDLLELRNSQGKYAQFLCDVCKFYLDWHTESYGAPVIFLHDPVSFAALV
RPELFTFKKGVVRVETQGICVGHTSMDMLLKKWNSENPWTGYSPISVAWT
VDVPKVVAFVKELVTKP
3D structure
PDB4kpo Structure and Function of Nucleoside Hydrolases from Physcomitrella patens and Maize Catalyzing the Hydrolysis of Purine, Pyrimidine, and Cytokinin Ribosides.
ChainA
Resolution2.49 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D8 D13 N37 P74 L123 A165 N166 H239 D240
Catalytic site (residue number reindexed from 1) D10 D15 N39 P76 L125 A167 N168 H241 D242
Enzyme Commision number 3.2.2.-
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 CA A D8 D13 L123 D240 D10 D15 L125 D242
Gene Ontology
Molecular Function
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0016799 hydrolase activity, hydrolyzing N-glycosyl compounds
GO:0046872 metal ion binding
Biological Process
GO:0006139 nucleobase-containing compound metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4kpo, PDBe:4kpo, PDBj:4kpo
PDBsum4kpo
PubMed24170203
UniProtB6T563

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