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3WZE

KDR in complex with ligand sorafenib

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 Residues18
DetailsBINDING SITE FOR RESIDUE BAX A 1201
ChainResidue
ALEU840
APHE918
ACYS919
ALYS920
AHIS1026
AILE1044
ACYS1045
AASP1046
APHE1047
AHOH3089
AVAL848
AALA866
AGLU885
AILE892
AVAL898
AVAL899
AVAL916
AGLU917

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 1202
ChainResidue
AGLN1011
AASN1040

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DTT A 1203
ChainResidue
AASP852
ACYS862
AHIS876

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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
APHE1078

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
ALEU840
ALYS868

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15962004, ECO:0000269|PubMed:18936167, ECO:0000269|PubMed:19136612
ChainResidueDetails
ATHR1001

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692
ChainResidueDetails
AARG1032
AILE1034

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:10102632, ECO:0000269|PubMed:18936167
ChainResidueDetails
AASP1046

site_idSWS_FT_FI6
Number of Residues1
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
ASER1104

site_idSWS_FT_FI7
Number of Residues1
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
AVAL1109

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PDB entries from 2024-11-06

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