Structure of PDB 2xba Chain A

Receptor sequence
>2xbaA (length=283) Species: 9606 (Homo sapiens) [Search protein sequence]
NYCFAGKTSSISDLKEVPRKNITLIRGLVYEGQVSPLQVAVKTLPEVCSE
QDELDFLMEALIISKFNHQNIVRCIGVSLQSLPRFILLELMAGGDLKSFL
RETRPRPSQPSSLAMLDLLHVARDIACGCQYLEENHFIHRDIAARNCLLT
CPGPGRVAKIGDFGMARDIYAMLPVKWMPPEAFMEGIFTSKTDTWSFGVL
LWEIFSLGYMPYPSKSNQEVLEFVTSGGRMDPPKNCPGPVYRIMTQCWQH
QPEDRPNFAIILERIEYCTQDPDVINTALPIEY
3D structure
PDB2xba Crystal Structures of Anaplastic Lymphoma Kinase in Complex with ATP Competitive Inhibitors.
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) D1249 A1251 R1253 N1254 D1270
Catalytic site (residue number reindexed from 1) D141 A143 R145 N146 D162
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 571 A A1148 K1150 L1196 E1197 L1198 M1199 A1200 G1202 R1253 L1256 Y1401 A40 K42 L88 E89 L90 M91 A92 G94 R145 L148 Y283 MOAD: Ki=23.68nM
PDBbind-CN: -logKd/Ki=7.63,Ki=23.68nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004713 protein tyrosine kinase activity
GO:0004714 transmembrane receptor protein tyrosine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation
GO:0007169 cell surface receptor protein tyrosine kinase signaling pathway
Cellular Component
GO:0016020 membrane

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2xba, PDBe:2xba, PDBj:2xba
PDBsum2xba
PubMed20695522
UniProtQ9UM73|ALK_HUMAN ALK tyrosine kinase receptor (Gene Name=ALK)

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