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6T2W

Crystal structure of the CSF1R kinase domain with a dihydropurinone inhibitor (compound 4)

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 Residues13
Detailsbinding site for residue M9T A 1001
ChainResidue
AVAL596
APHE797
AARG801
AHOH1102
AHOH1149
AALA614
ALYS616
ATHR663
AGLU664
ATYR665
ACYS666
AGLY669
ALEU785

site_idAC2
Number of Residues10
Detailsbinding site for residue SO4 A 1002
ChainResidue
AHIS655
AGLY656
AGLY656
AGLY656
AHOH1162
AHOH1162
AHOH1162
AHOH1252
AHOH1252
AHOH1252

site_idAC3
Number of Residues9
Detailsbinding site for residue SO4 A 1003
ChainResidue
ALYS595
ALYS619
ASER620
AGLN877
APRO882
ALYS883
AHOH1104
AHOH1123
AHOH1193

site_idAC4
Number of Residues6
Detailsbinding site for residue SO4 A 1004
ChainResidue
AARG676
AASN808
AASN854
AHOH1175
AHOH1183
AHOH1200

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 A 1005
ChainResidue
AGLN547
AARG549
ALYS551
AARG777

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
APRO824

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 Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20489731
ChainResidueDetails
ATYR546
AASP754
ALEU769
APRO855

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:P09581
ChainResidueDetails
ATYR561

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20489731, ECO:0007744|PubMed:19369195
ChainResidueDetails
AGLU745

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

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PDB entries from 2024-07-17

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