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

6HH1

Structure of c-Kit with allosteric inhibitor 3G8

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 Residues5
Detailsbinding site for residue PO4 A 1001
ChainResidue
AARG634
ATYR675
AGLU761
AHIS802
AGLY803

site_idAC2
Number of Residues13
Detailsbinding site for residue G4E A 1002
ChainResidue
AGLU671
ACYS673
ALEU799
AILE808
ACYS809
AASP810
APHE811
AHOH1132
AHOH1135
ALEU595
AVAL603
ALYS623
ALEU644

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGAFGKVVeAtaygliksdaamt.....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. GnHmNIVNLLGACT
ChainResidueDetails
AGLY648-THR661

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AASP572
APHE600
APRO627
ATYR675
AASP810

site_idSWS_FT_FI2
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
AASP572

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12824176, ECO:0000269|PubMed:9038210
ChainResidueDetails
ATHR574

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:7539802
ChainResidueDetails
ASER821

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20147452
ChainResidueDetails
ATYR823

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:12878163
ChainResidueDetails
ASER891

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12878163, ECO:0000269|PubMed:20147452
ChainResidueDetails
ATYR900

223532

PDB entries from 2024-08-07

PDB statisticsPDBj update infoContact PDBjnumon