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4YFI

TNNI3K complexed with inhibitor 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
C0004672molecular_functionprotein kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0004672molecular_functionprotein kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue 4CW A 801
ChainResidue
AILE469
AHOH914
AALA488
ALYS490
ATHR539
AGLN540
ATYR541
AILE542
ALEU595
AASP606

site_idAC2
Number of Residues8
Detailsbinding site for residue 4CW B 801
ChainResidue
BALA488
BGLU509
BTHR539
BGLN540
BILE542
BLEU595
BASP606
BHOH916

site_idAC3
Number of Residues12
Detailsbinding site for residue 4CW C 801
ChainResidue
CILE469
CVAL477
CALA488
CLYS490
CILE537
CTHR539
CGLN540
CTYR541
CILE542
CLEU595
CASP606
CHOH907

site_idAC4
Number of Residues9
Detailsbinding site for residue 4CW D 801
ChainResidue
DALA488
DGLU509
DILE522
DTHR539
DGLN540
DILE542
DLEU595
DASP606
DHOH913

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues22
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGSFGKVYkGrcrnki............VAIK
ChainResidueDetails
AILE469-LYS490

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AVAL487
BVAL487
CVAL487
DVAL487

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PDB entries from 2024-07-10

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