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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
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP740
BASP740

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE621
ALYS647
BILE621
BLYS647

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER769
ASER770
BSER769
BSER770

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PDB entries from 2024-09-11

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