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6MEP

Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with inhibitor UNC3437

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 Residues3
Detailsbinding site for residue CL A 901
ChainResidue
AARG584
ALEU587
ALEU589

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 902
ChainResidue
AILE650
AARG651
AARG732

site_idAC3
Number of Residues3
Detailsbinding site for residue CL A 903
ChainResidue
ATYR801
APRO802
ALYS820

site_idAC4
Number of Residues14
Detailsbinding site for residue 9VS A 904
ChainResidue
ALEU593
ALYS619
AMET641
AILE650
ALEU652
ALEU671
APRO672
AMET674
ALYS675
AASP678
AMET730
AASP741
APHE742
ALEU744

site_idAC5
Number of Residues2
Detailsbinding site for residue CL B 901
ChainResidue
BLEU819
BLYS820

site_idAC6
Number of Residues3
Detailsbinding site for residue CL B 902
ChainResidue
BARG584
BLEU587
BLEU589

site_idAC7
Number of Residues2
Detailsbinding site for residue MG B 903
ChainResidue
BASN728
BASP741

site_idAC8
Number of Residues18
Detailsbinding site for residue 9VS B 904
ChainResidue
BLEU593
BGLY594
BGLU595
BALA617
BLYS619
BMET641
BILE650
BARG651
BLEU652
BLEU671
BPRO672
BPHE673
BMET674
BLYS675
BGLY677
BMET730
BALA740
BASP741

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
BASP723

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU593
ALYS615
BLEU593
BLYS615

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:8702477
ChainResidueDetails
ATYR749
ATYR753
ATYR754
BTYR749
BTYR753
BTYR754

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PDB entries from 2024-07-17

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