Structure of PDB 1r0p Chain A

Receptor sequence
>1r0pA (length=301) Species: 9606 (Homo sapiens) [Search protein sequence]
TVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLD
KIHCAVKSLNRITDIGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSP
LVVLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKFLASKKFVHR
DLAARNCMLDEKFTVKVADFGLARDMYDKEFDSVHNKTGAKLPVKWMALE
SLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPITVYLLQGRRLLQPEYCP
DPLYEVMLKCWHPKAEMRPSFSELVSRISAIFSTFIGEHYVHVNATYVNV
K
3D structure
PDB1r0p Crystal structure of the tyrosine kinase domain of the hepatocyte growth factor receptor c-Met and its complex with the microbial alkaloid K-252a
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D1204 A1206 R1208 N1209 D1222 A1243
Catalytic site (residue number reindexed from 1) D151 A153 R155 N156 D169 A190
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 KSA A I1084 V1092 A1108 K1110 P1158 Y1159 M1160 M1211 R1227 M1229 Y1230 I35 V43 A55 K57 P105 Y106 M107 M158 R174 M176 Y177 MOAD: Kd=10nM
PDBbind-CN: -logKd/Ki=8.00,Kd=10nM
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1r0p, PDBe:1r0p, PDBj:1r0p
PDBsum1r0p
PubMed14559966
UniProtP08581|MET_HUMAN Hepatocyte growth factor receptor (Gene Name=MET)

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