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3PLS

RON in complex with ligand AMP-PNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1
ChainResidue
AHOH33
AASN1213
AASP1226
AANP1358
AHOH1359

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ANP A 1358
ChainResidue
AVAL1096
ALYS1114
APRO1162
ATYR1163
AMET1164
AASP1168
AARG1212
AASN1213
AMET1215
AASP1226
AMG1
AHOH33
AILE1088
AGLY1091

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGHFGVVYhGeyidqaqnriq.......CAIK
ChainResidueDetails
AILE1088-LYS1114

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCML
ChainResidueDetails
APHE1204-LEU1216

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:20726546
ChainResidueDetails
AASP1208

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AILE1088
ALYS1114
ALEU1161
AARG1212

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:15632155, ECO:0000305|PubMed:20726546
ChainResidueDetails
ATYR1238

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:15632155
ChainResidueDetails
ATYR1239

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15632155
ChainResidueDetails
ATYR1353

218853

PDB entries from 2024-04-24

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