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5D7V

Crystal structure of PTK6 kinase domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
C0004672molecular_functionprotein kinase activity
C0004713molecular_functionprotein tyrosine kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0004672molecular_functionprotein kinase activity
D0004713molecular_functionprotein tyrosine kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue PO4 A 501
ChainResidue
AGLU274
AARG277
AARG316

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 502
ChainResidue
AASP312
AARG316
AHIS345
ATRP353
AHOH618
AHOH642

site_idAC3
Number of Residues8
Detailsbinding site for residue GOL A 503
ChainResidue
AGLU235
AASN307
ATYR308
AILE309
AARG311
AGLY332
AARG335
AHOH664

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL A 504
ChainResidue
AARG311
AALA334
AILE337
AGLU339
ATYR342
ATYR364
AHOH607

site_idAC5
Number of Residues2
Detailsbinding site for residue PO4 B 501
ChainResidue
BARG277
BARG316

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL B 502
ChainResidue
BASP312
BARG316
BTYR342
BHIS345
BTRP353
BHOH618
BHOH650

site_idAC7
Number of Residues6
Detailsbinding site for residue GOL B 503
ChainResidue
BTYR308
BILE309
BARG311
BGLY332
BARG335
BHOH608

site_idAC8
Number of Residues5
Detailsbinding site for residue GOL B 504
ChainResidue
BARG311
BALA334
BARG335
BTYR364
BHOH606

site_idAC9
Number of Residues2
Detailsbinding site for residue PO4 C 501
ChainResidue
CARG277
CARG316

site_idAD1
Number of Residues7
Detailsbinding site for residue GOL C 502
ChainResidue
CASP312
CARG316
CHIS345
CTRP353
CHOH627
CHOH648
CHOH659

site_idAD2
Number of Residues5
Detailsbinding site for residue GOL C 503
ChainResidue
CARG311
CALA334
CILE337
CTYR342
CTYR364

site_idAD3
Number of Residues8
Detailsbinding site for residue GOL C 504
ChainResidue
CGLU235
CASN307
CTYR308
CILE309
CARG311
CGLY332
CARG335
CHOH651

site_idAD4
Number of Residues2
Detailsbinding site for residue PO4 D 501
ChainResidue
DARG277
DARG316

site_idAD5
Number of Residues5
Detailsbinding site for residue GOL D 502
ChainResidue
DASP312
DARG316
DHIS345
DHOH626
DHOH654

site_idAD6
Number of Residues7
Detailsbinding site for residue GOL D 503
ChainResidue
DGLU235
DTYR308
DILE309
DARG311
DGLY332
DARG335
DHOH621

site_idAD7
Number of Residues7
Detailsbinding site for residue GOL D 504
ChainResidue
DARG311
DALA334
DILE337
DGLU339
DTYR342
DTYR364
DHOH602

site_idAD8
Number of Residues12
Detailsbinding site for Di-peptide CXM B 184 and GLU B 185
ChainResidue
BARG186
BLYS240
BTYR251
BALA252
BVAL253
BVAL254
BSER255
BHOH601
BHOH611
BHOH623
BHOH659
DGLU281

site_idAD9
Number of Residues12
Detailsbinding site for Di-peptide CXM C 184 and GLU C 185
ChainResidue
AGLU281
ALEU410
AGLU411
CARG186
CLYS240
CTYR251
CALA252
CVAL253
CSER255
CHOH618
CHOH630
CHOH656

site_idAE1
Number of Residues9
Detailsbinding site for Di-peptide CXM D 184 and GLU D 185
ChainResidue
BGLU281
DARG186
DLYS240
DTYR251
DALA252
DVAL253
DSER255
DHOH609
DHOH648

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 Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP312
BASP312
CASP312
DASP312

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU197
BLEU197
CLEU197
DLEU197

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:27480927, ECO:0000305|PubMed:27993680
ChainResidueDetails
ALYS219
BLYS219
CLYS219
DLYS219

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12121988
ChainResidueDetails
ATYR342
ATYR351
BTYR342
BTYR351
CTYR342
CTYR351
DTYR342
DTYR351

218853

PDB entries from 2024-04-24

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