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7APG

Crystal structure of JAK3 in complex with FM587 (compound 9a)

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
C0004672molecular_functionprotein kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0004672molecular_functionprotein kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues28
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGNFGSVElCrydplgdntgal......VAVK
ChainResidueDetails
ALEU828-LYS855

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
AALA949
BALA949
CALA949
DALA949

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
CLEU828
CLYS855
DLEU828
DLYS855
ALYS855
BLEU828
BLYS855
ALEU828

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:18250158
ChainResidueDetails
CTYR904
CTYR939
DTYR904
DTYR939
ATYR939
BTYR904
BTYR939
ATYR904

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15831699
ChainResidueDetails
BTYR980
BTYR981
CTYR980
CTYR981
DTYR980
DTYR981
ATYR980
ATYR981

219869

PDB entries from 2024-05-15

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