Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7AB0

Apo crystal structure of the MerTK kinase domain

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 Residues2
Detailsbinding site for residue CL A 901
ChainResidue
APRO802
ALYS820

site_idAC2
Number of Residues4
Detailsbinding site for residue CL A 902
ChainResidue
AARG687
AARG687
AMET798
AHOH1079

site_idAC3
Number of Residues5
Detailsbinding site for residue CL A 903
ChainResidue
AHOH1049
AHOH1120
AARG651
AMET674
AARG732

site_idAC4
Number of Residues3
Detailsbinding site for residue CL A 904
ChainResidue
AARG584
AILE588
ALEU589

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
AASP723

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
ATYR749
ATYR753
ATYR754

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon