Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3WZD

KDR in complex with ligand lenvatinib

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 LEV A 1201
ChainResidue
AGLY841
AGLY922
ALEU1035
ACYS1045
AASP1046
APHE1047
AGOL1210
AHOH3001
AHOH3002
AHOH3003
AALA866
AGLU885
AILE888
AVAL899
AGLU917
APHE918
ACYS919
ALYS920

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE DTT A 1202
ChainResidue
ACYS1024
AILE1025

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DTT A 1203
ChainResidue
AASP852
ACYS862
AARG863
ATHR864

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DTT A 1204
ChainResidue
AILE1077
APHE1078
AASP1112
AGLU1113
ACYS1116

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE DTT A 1205
ChainResidue
ACYS1007
ALEU1164

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1206
ChainResidue
APHE921
ATYR927
ASER930
AHOH3014
AHOH3029

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1207
ChainResidue
AALA1020
AILE1084
AGLN1085
ATHR1152
APHE1153
ASER1154
AHOH3090

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1208
ChainResidue
ATRP1096
ASER1100
APRO1128
AASP1129
AHOH3129
AHOH3162

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1209
ChainResidue
APHE921
ASER1037
AGLU1038
ALYS1039
AASN1040
AHOH3082

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1210
ChainResidue
AARG1032
AASN1033
ACYS1045
AASP1046
ALEV1201
AHOH3001
AHOH3013

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1211
ChainResidue
AGLU1003
AHIS1004
ACYS1007
AASN1040

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

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon