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6CZ3

Structure of the PTK6 kinase domain bound to a type I inhibitor (3-fluoro-4-{[6-methyl-3-(1H-pyrazol-4-yl)imidazo[1,2-a]pyrazin-8-yl]amino}phenyl)(morpholin-4-yl)methanone

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 Residues14
Detailsbinding site for residue FLJ A 9001
ChainResidue
AARG195
AMET267
AALA268
AGLY270
ALYS282
AASP330
ALEU197
AVAL205
AALA217
ALYS219
ALEU248
ATHR264
AGLU265
ALEU266

site_idAC2
Number of Residues3
Detailsbinding site for residue ACT A 9002
ChainResidue
AARG223
AGLN229
AK9010

site_idAC3
Number of Residues7
Detailsbinding site for residue ACT A 9003
ChainResidue
AARG186
ATRP210
ALYS211
AARG213
ALYS338
AGLU339
AHOH9118

site_idAC4
Number of Residues2
Detailsbinding site for residue ACT A 9004
ChainResidue
AMET231
ALYS327

site_idAC5
Number of Residues3
Detailsbinding site for residue ACT A 9005
ChainResidue
AARG399
AALA402
ATYR404

site_idAC6
Number of Residues3
Detailsbinding site for residue ACT A 9006
ChainResidue
ASER360
AARG361
AASP401

site_idAC7
Number of Residues2
Detailsbinding site for residue ACT A 9007
ChainResidue
AGLU304
AASN307

site_idAC8
Number of Residues4
Detailsbinding site for residue ACT A 9008
ChainResidue
AASP212
ATYR351
AHIS394
AHOH9173

site_idAC9
Number of Residues3
Detailsbinding site for residue K A 9009
ChainResidue
AGLU189
APHE191
ATHR192

site_idAD1
Number of Residues3
Detailsbinding site for residue K A 9010
ChainResidue
AARG223
ALEU226
AACT9002

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues23
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGYFGEVFeGlwkdrvq...........VAIK
ChainResidueDetails
ALEU197-LYS219

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YIHrDLAARNILV
ChainResidueDetails
ATYR308-VAL320

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
AASP312

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU197

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:27480927, ECO:0000305|PubMed:27993680
ChainResidueDetails
ALYS219

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12121988
ChainResidueDetails
ATYR342
ATYR351

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PDB entries from 2024-04-17

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