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3KUL

Kinase domain of human ephrin type-A receptor 8 (EPHA8)

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 Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
AHOH11
AHOH104
AHOH298
AHIS693
AARG742
AARG749

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME A 401
ChainResidue
AALA668
AMET710
AGLU648
ACYS650
AILE666

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 403
ChainResidue
AHOH58
ATYR651
ATYR715
AMET716
AGLU717
AGLY719

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 910
ChainResidue
AHOH215
AARG884
ASER886
BARG884

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BME B 402
ChainResidue
BGLU648
BCYS650

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGDSGEVCyGrlrvpgqrdvp.......VAIK
ChainResidueDetails
AILE641-LYS667
BILE641-LYS667

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YVHrDLAARNVLV
ChainResidueDetails
ATYR756-VAL768
BTYR756-VAL768

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
BASP760

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BILE641
BLYS667

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:O09127
ChainResidueDetails
BTYR616
BTYR839

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BARG764
BASP760

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AARG764
AASP760

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BALA762
BASP760

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AALA762
AASP760

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASN765
BALA762
BASP760

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN765
AALA762
AASP760

236060

PDB entries from 2025-05-14

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