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

7KHJ

Crystal structure of KIT kinase domain with a small molecule inhibitor, PLX8512 in the DFG-in state

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0004714molecular_functiontransmembrane receptor protein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
A0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0004714molecular_functiontransmembrane receptor protein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue WEG A 1001
ChainResidue
AALA621
AASP810
ATHR670
AGLU671
ATYR672
ACYS673
ACYS674
ATYR675
AGLY676
ALEU799

site_idAC2
Number of Residues10
Detailsbinding site for residue WEG B 1001
ChainResidue
BLEU595
BTHR670
BTYR672
BCYS673
BCYS674
BTYR675
BGLY676
BLEU799
BCYS809
BASP810

Functional Information from PROSITE/UniProt
site_idPS00024
Number of Residues16
DetailsHEMOPEXIN Hemopexin domain signature. LPvkWmapEsIFNSVY
ChainResidueDetails
ALEU831-TYR846

site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGAFGKVVeAtaqgliksdaamt.....VAVK
ChainResidueDetails
ALEU595-LYS623

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNILL
ChainResidueDetails
ACYS788-LEU800

site_idPS00240
Number of Residues14
DetailsRECEPTOR_TYR_KIN_III Receptor tyrosine kinase class III signature. GnHeNIVNLLGACT
ChainResidueDetails
AGLY648-THR661

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
ASER850
BSER850

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING:
ChainResidueDetails
ATYR568
BLYS623
BGLU671
BSER854
BTYR855
BSER868
AGLY596
ALYS623
AGLU671
ASER854
ATYR855
ASER868
BTYR568
BGLY596

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:20147452
ChainResidueDetails
AHIS547
ATYR553
ACYS788
BHIS547
BTYR553
BCYS788

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12824176, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:21030588, ECO:0000269|PubMed:9038210
ChainResidueDetails
ATYR568
BTYR568

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12824176, ECO:0000269|PubMed:9038210
ChainResidueDetails
ATYR570
BTYR570

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:10377264, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:20147452
ChainResidueDetails
AGLU761
BGLU761

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:20147452, ECO:0000269|PubMed:9038210
ChainResidueDetails
AGLY779
BGLY779

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PKC/PRKCA => ECO:0000269|PubMed:7539802
ChainResidueDetails
ALEU799
AARG804
BLEU799
BARG804

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:7539802
ChainResidueDetails
APHE879
BPHE879

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20147452
ChainResidueDetails
ALYS881
BLYS881

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:12878163
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12878163, ECO:0000269|PubMed:20147452
ChainResidueDetails

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon