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7CQE

Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with AZD-7762

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
C0004672molecular_functionprotein kinase activity
C0004713molecular_functionprotein tyrosine kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue CL A 901
ChainResidue
AARG584
ALEU589

site_idAC2
Number of Residues2
Detailsbinding site for residue CL A 903
ChainResidue
ALEU819
ALYS820

site_idAC3
Number of Residues1
Detailsbinding site for residue CL A 904
ChainResidue
AARG818

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 905
ChainResidue
AGLN821
CTHR690

site_idAC5
Number of Residues11
Detailsbinding site for residue YDJ A 906
ChainResidue
APRO672
APHE673
AMET674
ALYS675
AARG727
AASN728
AMET730
AASP741
AHOH1004
ALEU593
AALA617

site_idAC6
Number of Residues3
Detailsbinding site for residue CL C 901
ChainResidue
CPRO802
CLEU819
CLYS820

site_idAC7
Number of Residues12
Detailsbinding site for residue YDJ C 902
ChainResidue
CVAL601
CALA617
CLYS619
CPRO672
CPHE673
CMET674
CLYS675
CARG727
CASN728
CMET730
CASP741
CHOH1005

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGEFGSVMeGnlkqedgtslk.......VAVK
ChainResidueDetails
ALEU593-LYS619

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FLHrDLAARNCML
ChainResidueDetails
APHE719-LEU731

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
AASP723
CASP723

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU593
ALYS615
CLEU593
CLYS615

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:8702477
ChainResidueDetails
ATYR749
ATYR753
ATYR754
CTYR749
CTYR753
CTYR754

224004

PDB entries from 2024-08-21

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