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5U6C

Crystal structure of the Mer kinase domain in complex with a macrocyclic inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0050660molecular_functionflavin adenine dinucleotide binding
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
B0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue 7YS A 9001
ChainResidue
ALEU593
AASP678
AARG727
AASN728
AMET730
AALA740
AHOH9151
AVAL601
AALA617
AMET650
ALEU671
APRO672
APHE673
AMET674
AGLY677

site_idAC2
Number of Residues14
Detailsbinding site for residue 7YS B 9001
ChainResidue
BLEU593
BVAL601
BALA617
BMET650
BPRO672
BPHE673
BMET674
BGLY677
BASP678
BARG727
BASN728
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

237992

PDB entries from 2025-06-25

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