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

5HNI

CRYSTAL STRUCTURE OF CMET WT with compound 3

Functional Information from GO Data
ChainGOidnamespacecontents
X0004672molecular_functionprotein kinase activity
X0004713molecular_functionprotein tyrosine kinase activity
X0005524molecular_functionATP binding
X0006468biological_processprotein phosphorylation
Y0004672molecular_functionprotein kinase activity
Y0004713molecular_functionprotein tyrosine kinase activity
Y0005524molecular_functionATP binding
Y0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue 63B X 1401
ChainResidue
XALA1108
XASP1222
XALA1226
XPRO1158
XTYR1159
XMET1160
XGLY1163
XASP1164
XARG1208
XASN1209
XALA1221

site_idAC2
Number of Residues12
Detailsbinding site for residue 63B Y 1401
ChainResidue
YVAL1092
YALA1108
YPRO1158
YTYR1159
YMET1160
YGLY1163
YASP1164
YARG1208
YASN1209
YMET1211
YASP1222
YALA1226

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGHFGCVYhGtlldndgkkih.......CAVK
ChainResidueDetails
XILE1084-LYS1110

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCML
ChainResidueDetails
XPHE1200-LEU1212

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
XLEU1186
YLEU1186

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
XVAL1066
YVAL1066

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
XVAL1092
YVAL1092

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:12475979
ChainResidueDetails
XLEU1212
XGLU1347
YLEU1212
YGLU1347

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979
ChainResidueDetails
XPHE1216
YPHE1216

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:1655790
ChainResidueDetails
XTHR1217
YTHR1217

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195
ChainResidueDetails
XVAL1271
YVAL1271

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:7513258
ChainResidueDetails
XSER1331
YSER1331

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15735664, ECO:0000269|PubMed:7513258
ChainResidueDetails
XSER1338
YSER1338

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon