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3CPB

Crystal structure of the VEGFR2 kinase domain in complex with a bisamide inhibitor

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
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0004714molecular_functiontransmembrane receptor protein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE C92 A 1
ChainResidue
AALA866
AASP1046
APHE1047
ALYS868
AGLU885
ATHR916
AGLU917
APHE918
ACYS919
ALEU1035
ACYS1045

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE C92 B 2
ChainResidue
BALA866
BLYS868
BGLU885
BTHR916
BGLU917
BPHE918
BCYS919
BLEU1035
BCYS1045
BASP1046
BPHE1047

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGAFGQVIeAdafgidktatcrt.....VAVK
ChainResidueDetails
ALEU840-LYS868

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNILL
ChainResidueDetails
ACYS1024-LEU1036

site_idPS00240
Number of Residues14
DetailsRECEPTOR_TYR_KIN_III Receptor tyrosine kinase class III signature. GhHlNVVNLLGACT
ChainResidueDetails
AGLY893-THR906

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP1028
BASP1028

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
ALEU840
ALYS868
BLEU840
BLYS868

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15962004, ECO:0000269|PubMed:18936167, ECO:0000269|PubMed:19136612
ChainResidueDetails
ATHR1001
BTHR1001

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692
ChainResidueDetails
AARG1032
AILE1034
BARG1032
BILE1034

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:10102632, ECO:0000269|PubMed:18936167
ChainResidueDetails
ATYR996
BTYR996

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:10037737, ECO:0000269|PubMed:10102632, ECO:0000269|PubMed:15215251, ECO:0000269|PubMed:15962004, ECO:0000269|PubMed:18936167
ChainResidueDetails
APTR1054
BPTR1054

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:10037737, ECO:0000269|PubMed:10102632, ECO:0000269|PubMed:10368301, ECO:0000269|PubMed:15215251, ECO:0000269|PubMed:15962004, ECO:0000269|PubMed:18936167
ChainResidueDetails
APTR1059
BPTR1059

220113

PDB entries from 2024-05-22

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