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4I5C

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
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE C5I A 1201
ChainResidue
ALEU881
AMET956
AGLU957
APHE958
ALEU959
AASN1008
ALEU1010
AGLY1020
AASP1021
AHOH1332
AHOH1356
AGLY882
AGLU883
AGLY884
AGLY887
ALYS888
AVAL889
AALA906
ALYS908

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 1201
ChainResidue
BARG879
BLEU881
BPRO960
BGLY962
BC5I1205

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 1202
ChainResidue
BASP866
BPRO867
BHIS869
BPHE870

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 1203
ChainResidue
BLEU875
BGLU890
BCYS892
BLYS953

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 1204
ChainResidue
AGLN1098
BGLY1097
BGLN1098

site_idAC6
Number of Residues20
DetailsBINDING SITE FOR RESIDUE C5I B 1205
ChainResidue
BLEU881
BGLY882
BGLU883
BGLY884
BGLY887
BLYS888
BVAL889
BALA906
BLYS908
BMET956
BGLU957
BPHE958
BLEU959
BARG1007
BASN1008
BLEU1010
BGLY1020
BASP1021
BEDO1201
BHOH1356

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 2024-05-01

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