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6VNL

JAK2 JH1 in complex with SG3-179

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
C0004672molecular_functionprotein kinase activity
C0004713molecular_functionprotein tyrosine kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0004672molecular_functionprotein kinase activity
D0004713molecular_functionprotein tyrosine kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue 5W2 D 1201
ChainResidue
DLEU855
DASN981
DLEU983
DASP994
DGLY856
DGLY858
DALA880
DGLU930
DLEU932
DGLY935
DASP939
DARG980

site_idAC2
Number of Residues12
Detailsbinding site for residue 5W2 B 1201
ChainResidue
BLEU855
BGLY856
BGLY858
BVAL863
BALA880
BLYS882
BMET929
BGLU930
BLEU932
BGLY935
BLEU983
BASP994

site_idAC3
Number of Residues14
Detailsbinding site for residue 5W2 C 1201
ChainResidue
CLEU855
CGLY856
CGLY858
CVAL863
CALA880
CGLU930
CTYR931
CLEU932
CGLY935
CASP939
CARG980
CASN981
CLEU983
CASP994

site_idAC4
Number of Residues14
Detailsbinding site for residue 5W2 A 1201
ChainResidue
ALEU855
AGLY856
AGLY858
AALA880
AGLU930
ATYR931
ALEU932
AGLY935
AASN981
ALEU983
AASP994
AHOH1306
AHOH1352
CASP1004

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGNFGSVEmCrydplqdntgevv.....AVKK
ChainResidueDetails
DLEU855-LYS883

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YIHrDLATRNILV
ChainResidueDetails
DTYR972-VAL984

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
DASP976
BASP976
CASP976
AASP976

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
DLEU855
DLYS882
BLEU855
BLYS882
CLEU855
CLYS882
ALEU855
ALYS882

site_idSWS_FT_FI3
Number of Residues12
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:Q62120
ChainResidueDetails
DTYR868
ATYR868
ATYR966
ATYR972
DTYR966
DTYR972
BTYR868
BTYR966
BTYR972
CTYR868
CTYR966
CTYR972

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16174768
ChainResidueDetails
DPTR1007
BPTR1007
CPTR1007
APTR1007

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:16174768
ChainResidueDetails
DTYR1008
BTYR1008
CTYR1008
ATYR1008

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PDB entries from 2024-06-26

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