Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6DKW

Crystal structure of Trk-A in complex with the Pan-Trk Kinase Inhibitor, compound 3.

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
A0016020cellular_componentmembrane
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
B0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue GXA A 801
ChainResidue
AVAL524
AMET592
AARG593
AGLY595
ALEU641
APHE646
AHIS648
ALEU657
AILE666
AGLY667
AASP668
AALA542
ALEU564
ALEU567
AILE572
AVAL573
APHE589
AGLU590
ATYR591

site_idAC2
Number of Residues16
Detailsbinding site for residue GXA B 801
ChainResidue
BLEU516
BALA542
BLEU564
BLEU567
BVAL573
BPHE589
BGLU590
BTYR591
BMET592
BARG593
BGLY595
BLEU641
BHIS648
BILE666
BGLY667
BASP668

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGKVFlAechnllpeqdkml.....VAVK
ChainResidueDetails
ALEU516-LYS544

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLATRNCLV
ChainResidueDetails
APHE646-VAL658

site_idPS00239
Number of Residues9
DetailsRECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYstdYYR
ChainResidueDetails
AASP674-ARG682

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
AASP650
BASP650

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU516
ALYS544
BLEU516
BLYS544

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Interaction with PLCG1
ChainResidueDetails
ATYR791
BTYR791

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:8155326
ChainResidueDetails
ATYR676
BTYR676

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15488758, ECO:0000269|PubMed:8155326
ChainResidueDetails
ATYR680
ATYR681
BTYR680
BTYR681

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15488758, ECO:0000269|PubMed:7510697, ECO:0000269|PubMed:8155326
ChainResidueDetails
ATYR791
BTYR791

224004

PDB entries from 2024-08-21

PDB statisticsPDBj update infoContact PDBjnumon