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3CJG

Crystal structure of VEGFR2 in complex with a 3,4,5-trimethoxy aniline containing pyrimidine

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 Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
ALYS824
AGLU826
APHE827
AILE854
ALYS856
ALEU900
AHOH1249

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 2
ChainResidue
ASER1102
AHOH1185
AHOH1259
AARG930
AALA1101

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE KIM A 1167
ChainResidue
ALEU838
ALYS866
AGLU883
AGLU915
APHE916
ACYS917
ALYS918
AGLY920
ALEU1033
AHOH1230
AHOH1233

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGAFGQVIeAdafgidktatcrt.....VAVK
ChainResidueDetails
ALEU838-LYS866

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNILL
ChainResidueDetails
ACSO1022-LEU1034

site_idPS00240
Number of Residues14
DetailsRECEPTOR_TYR_KIN_III Receptor tyrosine kinase class III signature. GhHlNVVNLLGACT
ChainResidueDetails
AGLY891-THR904

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"10102632","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18936167","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AARG1030
AASP1026

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP1026
AALA1028

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN1031
AASP1026
AALA1028

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PDB entries from 2025-08-27

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