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4YFF

TNNI3K complexed with inhibitor 2

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 Residues12
Detailsbinding site for residue 4CV A 801
ChainResidue
AILE469
ALEU595
AASP606
AHOH902
AALA488
ALYS490
AILE537
ATHR539
AGLN540
ATYR541
AILE542
AHIS592

site_idAC2
Number of Residues11
Detailsbinding site for residue 4CV B 801
ChainResidue
BALA488
BLYS490
BILE537
BTHR539
BGLN540
BTYR541
BILE542
BHIS592
BLEU595
BASP606
BHOH901

site_idAC3
Number of Residues12
Detailsbinding site for residue 4CV C 801
ChainResidue
CILE469
CALA488
CLYS490
CILE537
CTHR539
CGLN540
CTYR541
CILE542
CHIS592
CLEU595
CASP606
CHOH901

site_idAC4
Number of Residues11
Detailsbinding site for residue 4CV D 801
ChainResidue
DALA488
DLYS490
DILE537
DTHR539
DGLN540
DTYR541
DILE542
DHIS592
DLEU595
DASP606
DHOH903

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

219140

PDB entries from 2024-05-01

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