Structure of PDB 3brb Chain B

Receptor sequence
>3brbB (length=271) Species: 9606 (Homo sapiens) [Search protein sequence]
NKLEDVVIDRNLLILGKILGEGEFGSVMEGNLKQEDGTSLKVAVKTMKLD
NSSQREIEEFLSEAACMKDFSHPNVIRLLGVCIEMSSQGIPKPMVILPFM
KYGDLHTYLLYSRLETGPKHIPLQTLLKFMVDIALGMEYLSNRNFLHRDL
AARNCMLRDDMTVCVADFGLPVKWIAIESLADRVYTSKSDVWAFGVTMWE
IATRGMTPYPGVQNHEMYDYLLHGHRLKQPEDCLDELYEIMYSCWRTDPL
DRPTFSVLRLQLEKLLESLPD
3D structure
PDB3brb Structural insights into the inhibited states of the Mer receptor tyrosine kinase.
ChainB
Resolution1.9 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) D723 A725 R727 N728 D741
Catalytic site (residue number reindexed from 1) D149 A151 R153 N154 D167
Enzyme Commision number 2.7.10.1: receptor protein-tyrosine 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 CL B R687 M798 R113 M206
BS02 CL B R584 L589 R10 L15
BS03 CL B R651 R732 R77 R158
BS04 MG B N728 D741 N154 D167
BS05 ADP B A617 K619 F673 M674 M730 A43 K45 F99 M100 M156
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004713 protein tyrosine 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:3brb, PDBe:3brb, PDBj:3brb
PDBsum3brb
PubMed19028587
UniProtQ12866|MERTK_HUMAN Tyrosine-protein kinase Mer (Gene Name=MERTK)

[Back to BioLiP]