Structure of PDB 6cpt Chain A

Receptor sequence
>6cptA (length=519) Species: 5476 (Candida albicans) [Search protein sequence]
MAEVLSLVDLEIPQVTDKYYKFDTFKHLICHLFKKTSTETDSNVPIVIIF
PTTSKLDNLPFSDKSLLIQFFFTHLNILMIQGEGKLYQEISSAKELLTNR
ISRVGNWTGTTHFRSKIAGIIPTMTYILNCNATRSEIATNQLIYLYRLMI
EEINFIELLQDASTTRLSQLCYAVGHWSFPAHNLSNDDLVYCVYLMIDYA
IKQVEGFDNIPLNELLAFIFIVRDTYKNGNPFHNFRHAVDVLQACFHFLI
RLGSLPKFKQFVEDPKLDYTEVHDKHTVLIALKASLNPIQTLGLLVAALG
HDVGHPGTTNDFMIKFSAPTALLYNDRSVLESYHASLFINKVLRICWPDL
LTCTIEEKSELTIRSLIISSILATDMGEHNEYVNRLKSFKTILNHDNTVK
LISALLIKCADISNVTRPLRVSAQWAMVLSREFAEVELLKSVIKKDIDLD
FTKDLTYDDVPHELREILEIQPDIHKGQIFFINLFAENLFNSVSDLLPQL
QYTCDIIMENKLFWLERAK
3D structure
PDB6cpt Crystal Structures of Candida albicans Phosphodiesterase 2 and Implications for Its Biological Functions.
ChainA
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.1.4.-
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 ZN A H278 H349 D350 D462 H237 H301 D302 D411
BS02 IBM A N465 L480 F532 N414 L429 F481
Gene Ontology
Molecular Function
GO:0004114 3',5'-cyclic-nucleotide phosphodiesterase activity
GO:0004115 3',5'-cyclic-AMP phosphodiesterase activity
GO:0008081 phosphoric diester hydrolase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
GO:0047555 3',5'-cyclic-GMP phosphodiesterase activity
Biological Process
GO:0007165 signal transduction
GO:0019933 cAMP-mediated signaling
GO:0046069 cGMP catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6cpt, PDBe:6cpt, PDBj:6cpt
PDBsum6cpt
PubMed30231198
UniProtQ8NJP9

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