Structure of PDB 2biy Chain A

Receptor sequence
>2biyA (length=287) Species: 9606 (Homo sapiens) [Search protein sequence]
PQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKE
NKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYI
RKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQI
TDFGTAKVLSPESKQARANAFVGTAQYVSPELLTEKSACKSSDLWALGCI
IYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDA
TKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKL
3D structure
PDB2biy Role of T-loop phosphorylation in PDK1 activation, stability, and substrate binding.
ChainA
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D205 K207 E209 N210 D223 T245
Catalytic site (residue number reindexed from 1) D134 K136 E138 N139 D152 T174
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 ATP A G89 G91 S92 S94 V96 A109 K111 S160 A162 E166 L212 G18 G20 S21 S23 V25 A38 K40 S89 A91 E95 L141
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:2biy, PDBe:2biy, PDBj:2biy
PDBsum2biy
PubMed15741170
UniProtO15530|PDPK1_HUMAN 3-phosphoinositide-dependent protein kinase 1 (Gene Name=PDPK1)

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