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7AAY

Crystal structure of MerTK kinase domain in complex with Merestinib

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue L1X A 901
ChainResidue
AGLU595
APHE673
AMET674
ALEU714
APHE719
AHIS721
AMET730
AVAL739
AALA740
AASP741
APHE742
AVAL601
AALA617
ALYS619
AGLU637
AMET641
AILE650
ALEU671
APRO672

site_idAC2
Number of Residues4
Detailsbinding site for residue CL A 902
ChainResidue
APRO802
ALYS820
AHOH1003
AHOH1021

site_idAC3
Number of Residues3
Detailsbinding site for residue CL A 903
ChainResidue
AARG687
AARG687
AHOH1079

site_idAC4
Number of Residues5
Detailsbinding site for residue CL A 904
ChainResidue
AARG651
APRO672
AMET674
AARG732
AHOH1042

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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AARG727

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU593
ALYS615

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:8702477
ChainResidueDetails
ATYR753
AGLY757
AARG758

226707

PDB entries from 2024-10-30

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