Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5USY

JAK2 JH1 in complex with JNJ-7706621

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 Residues14
Detailsbinding site for residue SKE A 1201
ChainResidue
ALEU855
ALEU983
AHOH1337
AHOH1383
AHOH1494
BGLN853
AVAL863
AALA880
AMET929
AGLU930
ATYR931
ALEU932
APRO933
AGLY935

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 1202
ChainResidue
AGLN955
AGLN959
AARG1127
AHOH1306
AHOH1309
AHOH1389

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 1203
ChainResidue
AARG1090
AASP1092
AGLY1093

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL A 1204
ChainResidue
AGLU1052
ALYS1053
ASER1054
ALYS1055
ASER1056
AALA1059
AHOH1361

site_idAC5
Number of Residues8
Detailsbinding site for residue GOL A 1205
ChainResidue
AARG923
AGLU1080
ALYS1083
AHOH1317
AHOH1327
AHOH1469
AHOH1482
BLYS962

site_idAC6
Number of Residues14
Detailsbinding site for residue SKE B 1201
ChainResidue
AGLN853
BLEU855
BVAL863
BALA880
BMET929
BGLU930
BTYR931
BLEU932
BGLY935
BLEU983
BHOH1308
BHOH1327
BHOH1376
BHOH1521

site_idAC7
Number of Residues7
Detailsbinding site for residue SO4 B 1202
ChainResidue
AHOH1327
BGLN955
BGLN959
BARG1127
BHOH1312
BHOH1319
BHOH1351

site_idAC8
Number of Residues4
Detailsbinding site for residue SO4 B 1203
ChainResidue
BARG1090
BASP1092
BGLY1093
BHOH1442

site_idAC9
Number of Residues8
Detailsbinding site for residue SO4 B 1204
ChainResidue
BLYS1053
BSER1054
BLYS1055
BSER1056
BALA1059
BHOH1345
BHOH1346
BHOH1439

site_idAD1
Number of Residues5
Detailsbinding site for residue GOL B 1205
ChainResidue
BTYR918
BARG922
BLEU1026
BGLN1072
BVAL1075

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
ATYR1008
BTYR1008

220113

PDB entries from 2024-05-22

PDB statisticsPDBj update infoContact PDBjnumon