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5K0X

Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with inhibitor UNC2541

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 Residues2
Detailsbinding site for residue CL A 901
ChainResidue
AARG584
ALEU589

site_idAC2
Number of Residues2
Detailsbinding site for residue CL A 902
ChainResidue
APRO802
ALYS820

site_idAC3
Number of Residues3
Detailsbinding site for residue CL A 903
ChainResidue
AARG687
BMET798
BHOH1036

site_idAC4
Number of Residues10
Detailsbinding site for residue K0X A 904
ChainResidue
APRO672
APHE673
AMET674
ALYS675
AARG727
AASN728
AMET730
AASP741
ALEU593
AALA617

site_idAC5
Number of Residues3
Detailsbinding site for residue CL B 901
ChainResidue
BPRO802
BLYS820
BHOH1016

site_idAC6
Number of Residues4
Detailsbinding site for residue CL B 902
ChainResidue
BARG584
BLEU587
BILE588
BLEU589

site_idAC7
Number of Residues8
Detailsbinding site for residue K0X B 903
ChainResidue
BLEU593
BALA617
BPRO672
BMET674
BLYS675
BARG727
BASN728
BMET730

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 2024-04-24

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