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

3LPB

Crystal structure of Jak2 complexed with a potent 2,8-diaryl-quinoxaline 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 Residues18
DetailsBINDING SITE FOR RESIDUE NVB A 1133
ChainResidue
AHOH47
AGLU930
ATYR931
ALEU932
APRO933
AGLY935
AARG980
AASN981
ALEU983
AGLY993
AHOH202
AHOH252
ALEU855
AGLY856
ALYS857
AGLY858
AVAL863
AALA880

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE NVB B 1133
ChainResidue
BHOH122
BHOH148
BHOH223
BLEU855
BGLY856
BLYS857
BGLY858
BVAL863
BALA880
BGLU930
BTYR931
BLEU932
BPRO933
BGLY935
BARG980
BLEU983
BGLY993

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGNFGSVEmCrydplqdntgevv.....AVKK
ChainResidueDetails
ALEU855-LYS883

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YIHrDLATRNILV
ChainResidueDetails
ATYR972-VAL984

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
AASP976
BASP976

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BLEU855
BLYS882
ALEU855
ALYS882

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:Q62120
ChainResidueDetails
ATYR972
BTYR868
BTYR966
BTYR972
ATYR868
ATYR966

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16174768
ChainResidueDetails
APTR1007
BPTR1007

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:16174768
ChainResidueDetails
APTR1008
BPTR1008

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon