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

6IG8

Crystal structure of CSF-1R kinase domain with a small molecular inhibitor, JTE-952

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 Residues6
Detailsbinding site for residue MG A 1001
ChainResidue
AASP608
AGLU912
AHOH1142
AHOH1194
AHOH1263
AHOH1273

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 1002
ChainResidue
AHOH1374
AHOH1402
AHOH1421
AHOH1140
AHOH1146
AHOH1329

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL A 1003
ChainResidue
ALYS574
AGLY605
AHIS623
AASP625
AHOH1111
AHOH1112
AHOH1158

site_idAC4
Number of Residues18
Detailsbinding site for residue A7O A 1004
ChainResidue
ATRP550
AALA614
AMET637
ATHR663
AGLU664
ATYR665
ACYS666
ACYS667
AGLY669
ACYS774
AHIS776
AASN783
ALEU785
AGLY795
AASP796
APHE797
AHOH1184
AHOH1256

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGAFGKVVeAtafglgkedavlk.....VAVK
ChainResidueDetails
ALEU588-LYS616

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDVAARNVLL
ChainResidueDetails
ACYS774-LEU786

site_idPS00240
Number of Residues14
DetailsRECEPTOR_TYR_KIN_III Receptor tyrosine kinase class III signature. GqHeNIVNLLGACT
ChainResidueDetails
AGLY641-THR654

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
AASP778

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU588

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
ALYS616

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:P09581
ChainResidueDetails
ATYR561

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20489731, ECO:0007744|PubMed:19369195
ChainResidueDetails
AGLU745

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20489731
ChainResidueDetails
AASP754
ALEU769
ATYR809

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER759

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon