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6RSB

Structure based optimization of JAK1-ATP binding pocket Inhibitors in the aminopyrazole class

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 Residues23
Detailsbinding site for residue KGZ A 1201
ChainResidue
AARG879
ALYS908
AGLU957
APHE958
ALEU959
APRO960
AGLY962
AARG1007
AASN1008
ALEU1010
AGLY1020
ALEU881
AASP1021
AHOH1324
AHOH1337
AHOH1372
AGLY882
AGLY884
AHIS885
AGLY887
ALYS888
AVAL889
AALA906

site_idAC2
Number of Residues25
Detailsbinding site for residue KGZ B 1201
ChainResidue
BLEU881
BGLY882
BGLU883
BGLY884
BHIS885
BGLY887
BLYS888
BVAL889
BALA906
BLYS908
BSER909
BLEU910
BGLU957
BPHE958
BLEU959
BPRO960
BGLY962
BARG1007
BASN1008
BLEU1010
BGLY1020
BASP1021
BHOH1335
BHOH1377
BHOH1392

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP1003
BASP1003

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU881
BLEU881

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:32750333
ChainResidueDetails
ALYS908
BLYS908

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:11909529
ChainResidueDetails
APTR1034
APTR1035
BPTR1034
BPTR1035

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PDB entries from 2025-06-11

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