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4BI2

Scaffold Focused Virtual Screening: Prospective Application to the Discovery of TTK Inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1795
ChainResidue
ALYS529
AGLN541
AASN606
AZO81797

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 7PE A 1796
ChainResidue
AILE663
ASER537
ALYS553
ATYR568
AGLU571
AMET600

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ZO8 A 1797
ChainResidue
AILE531
AALA551
AILE586
AMET602
AGLU603
AGLY605
ALEU654
AEDO1795

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 1798
ChainResidue
ATRP622
ASER626

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues23
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGGSSKVFqVlnekkqi...........YAIK
ChainResidueDetails
AILE531-LYS553

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHsDLKpaNFLI
ChainResidueDetails
AILE643-ILE655

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:PRU10027
ChainResidueDetails
AASP647

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE531
ALYS553

226707

PDB entries from 2024-10-30

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