Structure of PDB 3dls Chain E

Receptor sequence
>3dlsE (length=282) Species: 9606 (Homo sapiens) [Search protein sequence]
AVELEGLAACEGEYSQKYSTMSPLGSGAFGFVWTAVDKEKNKEVVVKFIK
KEKVWIEDPKLGKVTLEIAILSRVEHANIIKVLDIFENQGFFQLVMEKHG
SGLDLFAFIDRHPRLDEPLASYIFRQLVSAVGYLRLKDIIHRDIKDENIV
IAEDFTIKLIDFGSAAYLERGKLFYTFCGTIEYCAPEVLMGNPYRGPELE
MWSLGVTLYTLVFEENPFCELEETVEAAIHPPYLVSKELMSLVSGLLQPV
PERRTTLEKLVTDPWVTQPVNLADYTWEEVFR
3D structure
PDB3dls Structural bases of PAS domain-regulated kinase (PASK) activation in the absence of activation loop phosphorylation.
ChainE
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D1128 K1130 E1132 N1133 D1146 L1153 T1165
Catalytic site (residue number reindexed from 1) D143 K145 E147 N148 D161 L168 T180
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 MG E N1133 D1146 N148 D161
BS02 ADP E G1006 V1013 V1026 K1028 I1065 H1084 G1087 D1089 V1135 I1145 D1146 G25 V32 V45 K47 I80 H99 G102 D104 V150 I160 D161
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3dls, PDBe:3dls, PDBj:3dls
PDBsum3dls
PubMed20943661
UniProtQ96RG2|PASK_HUMAN PAS domain-containing serine/threonine-protein kinase (Gene Name=PASK)

[Back to BioLiP]