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6GLB

Crystal structure of JAK3 in complex with Compound 20 (FM484)

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
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue F48 A 1201
ChainResidue
ALEU828
AHOH1301
AVAL836
AALA853
AGLU903
ATYR904
ALEU905
AARG953
AASN954
ALEU956

site_idAC2
Number of Residues7
Detailsbinding site for residue PHU A 1202
ChainResidue
ATRP1011
APRO1030
AMET1037
AARG1059
ALEU1060
ATRP1078
AHOH1333

site_idAC3
Number of Residues4
Detailsbinding site for residue EDO A 1203
ChainResidue
ALYS823
AARG840
AASN847
BPRO1093

site_idAC4
Number of Residues6
Detailsbinding site for residue EDO A 1204
ChainResidue
ALEU875
ALYS876
ALEU878
AHIS879
ALYS885
ATYR886

site_idAC5
Number of Residues2
Detailsbinding site for residue EDO A 1205
ChainResidue
AGLN1058
AARG1059

site_idAC6
Number of Residues9
Detailsbinding site for residue F48 B 1201
ChainResidue
BLEU828
BVAL836
BALA853
BGLU903
BTYR904
BLEU905
BARG953
BASN954
BLEU956

site_idAC7
Number of Residues7
Detailsbinding site for residue PHU B 1202
ChainResidue
BPHE992
BTRP1011
BMET1037
BARG1059
BLEU1060
BTRP1078
BHOH1324

site_idAC8
Number of Residues5
Detailsbinding site for residue EDO B 1203
ChainResidue
BLYS823
BILE825
BARG840
BASN847
BARG984

site_idAC9
Number of Residues6
Detailsbinding site for residue EDO B 1204
ChainResidue
BARG920
BPRO996
BLEU1054
BGLU1055
BARG1059
BPRO1080

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AALA949
BALA949

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU828
ALYS855
BLEU828
BLYS855

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:18250158
ChainResidueDetails
ATYR904
ATYR939
BTYR904
BTYR939

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15831699
ChainResidueDetails
ATYR980
ATYR981
BTYR980
BTYR981

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PDB entries from 2024-08-07

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