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5KHW

Crystal structure of JAK1 in complex with ADP

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 Residues17
Detailsbinding site for residue ADP A 1201
ChainResidue
ALEU881
ALEU959
AGLU966
AARG1007
AASN1008
AASP1021
AMG1202
AHOH1316
AHOH1322
AGLY882
AVAL889
AALA906
ALYS908
AVAL938
AMET956
AGLU957
APHE958

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 1202
ChainResidue
AASN1008
AASP1021
AADP1201

site_idAC3
Number of Residues19
Detailsbinding site for residue ADP B 1201
ChainResidue
BLEU881
BGLY882
BVAL889
BALA906
BLYS908
BVAL938
BMET956
BGLU957
BPHE958
BLEU959
BGLU966
BARG1007
BASN1008
BASP1021
BMG1202
BHOH1301
BHOH1302
BHOH1307
BHOH1311

site_idAC4
Number of Residues3
Detailsbinding site for residue MG B 1202
ChainResidue
BASN1008
BASP1021
BADP1201

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 2024-04-24

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