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3TCP

Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with inhibitor UNC569

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 Residues9
DetailsBINDING SITE FOR RESIDUE CKJ A 1
ChainResidue
AVAL601
AALA617
APRO672
AMET674
ALYS675
AGLY677
AARG727
AASN728
AMET730

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 865
ChainResidue
ALYS820

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA A 12
ChainResidue
AASP843
BASP843

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CA A 13
ChainResidue
AASP827

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CKJ B 2
ChainResidue
BALA617
BPRO672
BMET674
BLYS675
BGLY677
BARG727
BASN728
BMET730

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 865
ChainResidue
BHOH66
BARG687

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 3
ChainResidue
BPRO802
BLYS820

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA B 11
ChainResidue
BHOH61
BGLN821
BASP827

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
BLEU593
BLYS615
ALEU593
ALYS615

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

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PDB entries from 2024-04-17

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