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6C7Y

Crystal structure of inhibitory protein SOCS1 in complex with JAK1 kinase domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue ADP A 1201
ChainResidue
AGLY882
AGLU957
ALEU959
ASER963
AGLU966
AARG1007
AASN1008
ALEU1010
AASP1021
AMG1202
AMG1203
AGLY884
AHIS885
APHE886
AGLY887
AVAL889
AALA906
ALYS908
AMET956

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 1202
ChainResidue
AASN1008
AASP1021
AADP1201
AMG1203
AHOH1302
AHOH1317

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 1203
ChainResidue
AASP1003
AASP1021
AADP1201
AMG1202
AHOH1325

site_idAC4
Number of Residues10
Detailsbinding site for residue EDO A 1204
ChainResidue
ALEU1108
ALEU1108
ALYS1109
ALYS1109
AGLY1111
AGLY1111
AARG1113
AARG1113
APHE1134
APHE1134

site_idAC5
Number of Residues6
Detailsbinding site for residue EDO A 1205
ChainResidue
AGLN1055
ALYS1057
AHOH1316
BARG59
BSER60
BGLN61

site_idAC6
Number of Residues3
Detailsbinding site for residue EDO B 201
ChainResidue
AGLN1098
BARG59
BASP63

site_idAC7
Number of Residues4
Detailsbinding site for residue ACT B 202
ChainResidue
BVAL86
BARG104
BSER106
BTHR107

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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP1003

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU881

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:32750333
ChainResidueDetails
ALYS908

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:11909529
ChainResidueDetails
ATYR1034
APTR1035

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PDB entries from 2025-06-11

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