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2YN8

ephB4 kinase domain inhibitor complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE STU A 1889
ChainResidue
AILE621
AMET696
AGLY699
AARG744
ALEU747
ASER757
AASP758
AHOH2127
BMET687
AGLY622
AALA623
AALA645
ALYS647
AGLU664
ATHR693
AGLU694
APHE695

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE STU B 1889
ChainResidue
BILE621
BGLY622
BALA623
BALA645
BLYS647
BGLU664
BTHR693
BGLU694
BPHE695
BMET696
BGLY699
BARG744
BLEU747
BSER757
BASP758

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGAGEFGEVCrGrlkapgkkesc.......VAIK
ChainResidueDetails
AILE621-LYS647

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YVHrDLAARNILV
ChainResidueDetails
ATYR736-VAL748

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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