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

7KHG

Crystal structure of KIT kinase domain with a small molecule inhibitor, PLX3397

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
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue P31 A 1001
ChainResidue
ATRP557
ALEU783
AHIS790
ALEU799
AILE808
ACYS809
AASP810
AALA621
ALYS623
AGLU640
AILE653
AVAL654
ATHR670
AGLU671
ACYS673

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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
ASER850

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING:
ChainResidueDetails
ATYR568
AGLY596
ALYS623
AGLU671
ASER854
ATYR855
ASER868

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:20147452
ChainResidueDetails
AHIS547
ATYR553
ACYS788

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12824176, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:21030588, ECO:0000269|PubMed:9038210
ChainResidueDetails
ATYR568

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12824176, ECO:0000269|PubMed:9038210
ChainResidueDetails
ATYR570

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:10377264, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:20147452
ChainResidueDetails
AGLU761

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:20147452, ECO:0000269|PubMed:9038210
ChainResidueDetails
AGLY779

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKC/PRKCA => ECO:0000269|PubMed:7539802
ChainResidueDetails
ALEU799
AARG804

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:7539802
ChainResidueDetails
APHE879

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20147452
ChainResidueDetails
ALYS881

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:12878163
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12878163, ECO:0000269|PubMed:20147452
ChainResidueDetails

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon