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3LMG

Crystal structure of the ERBB3 kinase domain in complex with AMP-PNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 202
ChainResidue
AANP301
AASN820
AASP833

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ANP A 301
ChainResidue
AVAL704
ACYS721
ALYS723
ATHR768
AGLN769
ATYR770
ALEU771
ASER775
AASN815
AARG819
AASN820
ALEU822
AASP833
AMG202
ALEU696
ASER698
AGLY699
AVAL700
AGLY702

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 202
ChainResidue
BANP301
BASN820
BASP833

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ANP B 301
ChainResidue
BMG202
BLEU696
BGLY697
BSER698
BGLY699
BVAL700
BGLY702
BVAL704
BCYS721
BLYS723
BGLN769
BTYR770
BLEU771
BASN815
BARG819
BASN820
BLEU822
BASP833

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AASN815
BASN815

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
ALEU696
ALYS723
AGLN769
AASN815
BLEU696
BLYS723
BGLN769
BASN815

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER667
BSER667

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER963
BSER963

226707

PDB entries from 2024-10-30

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