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4EHZ

The Jak1 kinase domain in complex with inhibitor

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
C0004672molecular_functionprotein kinase activity
C0004713molecular_functionprotein tyrosine kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0004672molecular_functionprotein kinase activity
D0004713molecular_functionprotein tyrosine kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE JAK A 1201
ChainResidue
ALEU881
AASN1008
ALEU1010
AEDO1202
AHOH1304
AHOH1336
AVAL889
AALA906
AGLU957
APHE958
ALEU959
AGLY962
AGLU966
AARG1007

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1202
ChainResidue
AARG879
APRO960
AGLY962
AJAK1201
AHOH1432

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1203
ChainResidue
ALEU977
AGLN980
ALEU1075
ATYR1077
APRO1118

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 1204
ChainResidue
APRO867
AHIS869
APHE870

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 1205
ChainResidue
ALEU875
AGLU890
ALYS953

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1206
ChainResidue
AASN976
ALYS978
AGLN979
ALYS982
AHOH1414

site_idAC7
Number of Residues14
DetailsBINDING SITE FOR RESIDUE JAK B 1201
ChainResidue
BLEU881
BVAL889
BALA906
BGLU957
BPHE958
BLEU959
BGLY962
BGLU966
BARG1007
BASN1008
BLEU1010
BHOH1314
BHOH1317
BHOH1424

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 1202
ChainResidue
BGLU890
BVAL907
BLYS953
BHOH1329

site_idAC9
Number of Residues14
DetailsBINDING SITE FOR RESIDUE JAK C 1201
ChainResidue
CLEU881
CVAL889
CALA906
CGLU957
CPHE958
CLEU959
CGLY962
CGLU966
CARG1007
CASN1008
CLEU1010
CEDO1202
CHOH1302
CHOH1306

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO C 1202
ChainResidue
CARG879
CLEU881
CPRO960
CGLY962
CJAK1201
CHOH1448

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO C 1203
ChainResidue
CGLN1098

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO C 1204
ChainResidue
CLEU977
CGLN980
CLEU1075
CTYR1077
CHOH1375

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO C 1205
ChainResidue
CASP1040
CSER1043
CTYR1048
CCYS1052
CSER1056
CPHE1058
DMET1099

site_idBC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE JAK D 1201
ChainResidue
DHOH1302
DHOH1306
DLEU881
DVAL889
DALA906
DGLU957
DPHE958
DLEU959
DGLY962
DGLU966
DARG1007
DASN1008
DLEU1010
DGLY1020
DEDO1202

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO D 1202
ChainResidue
DARG879
DPRO960
DGLY962
DJAK1201
DHOH1386

site_idBC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO D 1203
ChainResidue
DASP866
DPRO969
DLYS970
DASN971
DLYS972
DASN973
DHOH1368
DHOH1392

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues28
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGHFGKVElCrydpegdntgeq......VAVK
ChainResidueDetails
ALEU881-LYS908

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YVHrDLAARNVLV
ChainResidueDetails
ATYR999-VAL1011

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
AASP1003
BASP1003
CASP1003
DASP1003

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU881
BLEU881
CLEU881
DLEU881

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:32750333
ChainResidueDetails
ALYS908
BLYS908
CLYS908
DLYS908

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:11909529
ChainResidueDetails
APTR1034
APTR1035
BPTR1034
BPTR1035
CPTR1034
CPTR1035
DPTR1034
DPTR1035

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PDB entries from 2024-05-01

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