Structure of PDB 5ncl Chain A

Receptor sequence
>5nclA (length=418) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
MYFERRPDLLTKGTQDKAAAVKLKIENFYQSSVKYAIERNERRVELETEL
TSHNWSEERKSRQLSSLGKKESQFLRLRRTRLSLEDFHTVKVIGKGAFGE
VRLVQKKDTGKIYAMKTLLKSEMYKKSDSPWVVSLYYSFQDAQYLYLIME
FLPGGDLMTMLIRWQLFTEDVTRFYMAECILAIETIHKLGFIHRAIKPDN
ILIDIRGHIKLSDFGLSTGFHKTHDSNYYSISLTMSNRQQIQTWRKSRRL
MAYSTVGTPDYIAPEIFLYQGYGQECDWWSLGAIMYECLIGWPPFCSETP
QETYRKIMNFEQTLQFPDDIHISYEAEDLIRRLLTHADQRLGRHGGADEI
KSHPFFRGVDWNTIRQVEAPYIPKLSSITDTRFFPTDELENVPDSPAMLP
FIGYTYSRFDYLTRKNAL
3D structure
PDB5ncl Ndr/Lats Kinases Bind Specific Mob-Family Coactivators through a Conserved and Modular Interface.
ChainA
Resolution3.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A475 K477 N480 D493 S563 T574
Catalytic site (residue number reindexed from 1) A195 K197 N200 D213 S247 T258
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein kinase.
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 peptide A D450 R453 F454 G674 P686 D170 R173 F174 G358 P370
BS02 ANP A I358 V366 K381 L432 D436 D479 N480 L482 T498 F700 I93 V101 K116 L152 D156 D199 N200 L202 T218 F384
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:5ncl, PDBe:5ncl, PDBj:5ncl
PDBsum5ncl
PubMed32250593
UniProtP53894|CBK1_YEAST Serine/threonine-protein kinase CBK1 (Gene Name=CBK1)

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