Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6PE6

PANK3 complex structure with compound PZ-3022

Functional Information from GO Data
ChainGOidnamespacecontents
A0004594molecular_functionpantothenate kinase activity
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0015937biological_processcoenzyme A biosynthetic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0019842molecular_functionvitamin binding
A0042803molecular_functionprotein homodimerization activity
A1905502molecular_functionacetyl-CoA binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue ODG A 401
ChainResidue
AGLU138
AARG306
AALA337
ALEU338
ATRP341
AVAL194
AARG207
AGLY210
ATHR211
AVAL268
AASN299
AGLY302
ASER303

site_idAC2
Number of Residues26
Detailsbinding site for residue ANP A 402
ChainResidue
AGLY19
AGLY20
ATHR21
ALEU22
ALYS24
AGLU138
AGLY191
ASER192
AGLY215
AGLY216
APHE231
AILE253
AGLY321
AASN322
APHE323
AARG325
AMG403
AHOH502
AHOH535
AHOH542
AHOH546
AHOH553
AHOH563
AHOH565
AHOH582
AHOH641

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 403
ChainResidue
AANP402
AHOH535
AHOH546
AHOH553
AHOH560

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:27555321
ChainResidueDetails
AGLU138

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:17631502
ChainResidueDetails
ASER192

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17631502, ECO:0000269|PubMed:20797618
ChainResidueDetails
ASER195
AARG207

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon