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3LCD

Inhibitor Bound to A DFG-In structure of the Kinase Domain of CSF-1R

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 Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
ATYR668
AASN788
AGLY789

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 2
ChainResidue
AALA815
AARG777
AARG801
ATYR809
AVAL811
ALYS812
AGLY813

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE BDY A 923
ChainResidue
AHOH14
AHOH47
AHOH65
ALEU588
AVAL596
AALA614
AGLU664
ATYR665
ACYS666
ATYR668
AGLY669
AARG782
ALEU785
AASP796

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 Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20489731
ChainResidueDetails
ATYR546
AALA767
AARG782
ATYR809

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
APHE758

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ALYS772

218853

PDB entries from 2024-04-24

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