Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4V0G

JAK3 in complex with a covalent EGFR 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 Residues12
DetailsBINDING SITE FOR RESIDUE G9B A 2099
ChainResidue
ALEU828
AASP912
AARG953
AASP967
AALA853
AMET902
AGLU903
ATYR904
ALEU905
APRO906
AGLY908
ACYS909

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE G9B B 2099
ChainResidue
BALA853
BMET902
BGLU903
BTYR904
BLEU905
BPRO906
BGLY908
BCYS909
BASP912
BASP967

site_idAC3
Number of Residues10
DetailsBinding site for residues PTR A 980 and PTR A 981
ChainResidue
AARG870
ALYS972
ALEU973
APRO975
ALYS978
AASP979
AVAL982
AVAL983
AILE1003
APHE1004

site_idAC4
Number of Residues8
DetailsBinding site for residues PTR B 980 and PTR B 981
ChainResidue
BLYS972
BLEU973
BPRO975
BLYS978
BASP979
BVAL982
BILE1003
BPHE1004

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues28
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGNFGSVElCrydplgdntgal......VAVK
ChainResidueDetails
ALEU828-LYS855
BLEU828-LYS855

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CVHrDLAARNILV
ChainResidueDetails
ACYS945-VAL957
BCYS945-VAL957

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
BASP949

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BLEU828
BLYS855

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:18250158
ChainResidueDetails
BTYR904
BTYR939

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15831699
ChainResidueDetails
BPTR980
BPTR981

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon