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3FUP

Crystal structures of JAK1 and JAK2 inhibitor complexes

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 Residues15
DetailsBINDING SITE FOR RESIDUE MI1 A 1
ChainResidue
AHOH3
ATYR931
ALEU932
AARG980
ALEU983
AGLY993
AASP994
ALEU855
AGLY856
ALYS857
AGLY858
AGLY861
AVAL863
AALA880
AGLU930

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE MI1 B 1
ChainResidue
BHOH16
BGLY856
BLYS857
BGLY858
BGLY861
BSER862
BVAL863
BALA880
BMET929
BGLU930
BLEU932
BARG980
BLEU983
BGLY993
BASP994

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGNFGSVEmCrydplqdntgevv.....AVKK
ChainResidueDetails
ALEU855-LYS883

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YIHrDLATRNILV
ChainResidueDetails
ATYR972-VAL984

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP976
BASP976

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU855
ALYS882
BLEU855
BLYS882

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:Q62120
ChainResidueDetails
ATYR868
ATYR966
ATYR972
BTYR868
BTYR966
BTYR972

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16174768
ChainResidueDetails
APTR1007
BPTR1007

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:16174768
ChainResidueDetails
APTR1008
BPTR1008

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AARG980
AASP976

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BARG980
BASP976

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AALA978
AASP976

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BALA978
BASP976

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AALA978
AASN981
AASP976

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BALA978
BASN981
BASP976

224572

PDB entries from 2024-09-04

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