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4PMT

The structure of TrkA kinase bound to the inhibitor N~4~-(4-morpholin-4-ylphenyl)-N~6~-(pyridin-3-ylmethyl)pyrido[3,2-d]pyrimidine-4,6-diamine

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
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue 31Y A 801
ChainResidue
AGLU515
AARG654
ALEU657
AARG673
AHOH988
ALEU516
ALEU516
AGLY517
AALA542
APHE589
AGLU590
AMET592
AARG599

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 802
ChainResidue
AALA758
AARG761
AHOH903

site_idAC3
Number of Residues5
Detailsbinding site for residue ACT A 803
ChainResidue
AGLY625
AARG649
AARG702
AHOH905
AHOH910

site_idAC4
Number of Residues4
Detailsbinding site for residue ACT A 804
ChainResidue
AARG602
ATYR676
ALYS725
AGLN726

site_idAC5
Number of Residues4
Detailsbinding site for residue ACT A 805
ChainResidue
ALYS725
ATYR729
APRO749
AHOH971

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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP650

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU516
ALYS544

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:8155326
ChainResidueDetails
ATYR676

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15488758, ECO:0000269|PubMed:8155326
ChainResidueDetails
ATYR680
ATYR681

226707

PDB entries from 2024-10-30

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