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1YVJ

Crystal structure of the Jak3 kinase domain in complex with a staurosporine analogue

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DTV A 2962
ChainResidue
APHE833
ALYS855
AASP967
AGLY969
AGLN988

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DTV A 2963
ChainResidue
AHOH2116
AHOH2120
AHOH2146
AARG943
ALEU973
AHOH2094
AHOH2099

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 4ST A 2000
ChainResidue
ALEU828
AGLY829
AVAL836
AALA853
AHIS859
AMET902
AGLU903
ATYR904
ALEU905
AGLY908
AARG911
AARG953
ALEU956
AASP967
AHOH2052

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues28
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGNFGSVElCrydplgdntgal......VAVK
ChainResidueDetails
ALEU828-LYS855

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CVHrDLAARNILV
ChainResidueDetails
ACYS945-VAL957

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP949

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALYS855
ALEU828

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:18250158
ChainResidueDetails
ATYR939
ATYR904

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15831699
ChainResidueDetails
APTR980
APTR981

218500

PDB entries from 2024-04-17

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