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6MWE

CRYSTAL STRUCTURE OF TIE2 IN COMPLEX WITH DECIPERA COMPOUND DP1919

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue SO4 A 1201
ChainResidue
AARG999
ACYS1044
AALA1045
AHOH1302
BHIS881
BTYR954
BLYS958

site_idAC2
Number of Residues2
Detailsbinding site for residue SO4 A 1202
ChainResidue
AGLN939
AHIS943

site_idAC3
Number of Residues19
Detailsbinding site for residue 919 A 1203
ChainResidue
AILE830
AALA853
ALYS855
AGLU872
AVAL875
ALEU876
AILE885
AILE886
AGLU903
AALA905
AGLY908
AALA981
AASP982
APHE983
AGLY984
AARG987
AGLN989
AHOH1376
AHOH1401

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 B 1201
ChainResidue
ATYR1015
AHOH1325
BARG950
BASN1093

site_idAC5
Number of Residues2
Detailsbinding site for residue SO4 B 1202
ChainResidue
BGLN939
BHIS943

site_idAC6
Number of Residues20
Detailsbinding site for residue 919 B 1203
ChainResidue
BILE830
BALA853
BLYS855
BGLU872
BLEU876
BILE885
BILE886
BILE902
BGLU903
BTYR904
BALA905
BPHE960
BILE980
BALA981
BASP982
BPHE983
BGLY984
BARG987
BGLN989
BHOH1383

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues26
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGNFGQVLkArikkdglrmd........AAIK
ChainResidueDetails
AILE830-LYS855

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FIHrDLAARNILV
ChainResidueDetails
APHE960-VAL972

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:11080633
ChainResidueDetails
AASP964
BASP964

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
BILE830
BLYS855
AILE830
ALYS855

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:11513602
ChainResidueDetails
ATYR1108
BTYR860
BTYR992
BTYR1108
ATYR860
ATYR992

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14665640, ECO:0000269|PubMed:27270174
ChainResidueDetails
ATYR1102
BTYR1102

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PDB entries from 2024-06-12

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