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6IN0

Crystal structure of EphA3 in complex with 18-Crown-6

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue CL A 1001
ChainResidue
AILE788
AARG789

site_idAC2
Number of Residues4
Detailsbinding site for residue CL A 1002
ChainResidue
ALEU616
AASP617
AASN620
AHOH1227

site_idAC3
Number of Residues7
Detailsbinding site for residue O4B A 1003
ChainResidue
AMET674
AILE697
ASER763
AHOH1219
APHE632
ALYS653
AGLU670

site_idAC4
Number of Residues1
Detailsbinding site for residue O4B A 1004
ChainResidue
ALYS646

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGAGEFGEVCsGrlklpskkeis.......VAIK
ChainResidueDetails
AVAL627-LYS653

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YVHrDLAARNILI
ChainResidueDetails
ATYR742-ILE754

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
AASP746

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
ALYS653
AGLU700
AARG750
AGLY628

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:18547520
ChainResidueDetails
ATYR701

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:11870224
ChainResidueDetails
ATYR779

219869

PDB entries from 2024-05-15

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