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5DA3

Crystal structure of PTK6 Kinase domain with inhibitor

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 Residues8
Detailsbinding site for residue GOL A 501
ChainResidue
AASP312
AARG316
AHIS345
ATRP353
AHOH681
AHOH688
AHOH759
AHOH762

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 502
ChainResidue
AALA334
AILE337
AGLU339
ATYR342
AHOH719
AARG311

site_idAC3
Number of Residues16
Detailsbinding site for residue 58V A 503
ChainResidue
AARG195
ALEU197
AALA217
ALYS219
ALEU248
ATHR264
AGLU265
AMET267
AALA268
AGLY270
ALEU319
AASP330
AGLN430
AHOH609
AHOH622
AHOH753

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

222624

PDB entries from 2024-07-17

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