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6IBX

Human PFKFB3 in complex with a N-Aryl 6-Aminoquinoxaline inhibitor 5

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003873molecular_function6-phosphofructo-2-kinase activity
A0005524molecular_functionATP binding
A0006000biological_processfructose metabolic process
A0006003biological_processfructose 2,6-bisphosphate metabolic process
Functional Information from PROSITE/UniProt
site_idPS00175
Number of Residues10
DetailsPG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LcRHGEnEhN
ChainResidueDetails
ALEU250-ASN259

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255
ChainResidueDetails
APHE139
AILE169

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Tele-phosphohistidine intermediate => ECO:0000269|PubMed:22275052
ChainResidueDetails
ASER268

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:22275052
ChainResidueDetails
AARG337

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:16316985, ECO:0000269|PubMed:17499765, ECO:0000269|PubMed:22275052
ChainResidueDetails
AARG56
AASN178
ACYS439

site_idSWS_FT_FI5
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:16316985
ChainResidueDetails
APRO89
ALEU113
ALYS141
AALA147
AMET183
ALYS204
AASP208

site_idSWS_FT_FI6
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:25849762
ChainResidueDetails
AASP267
AGLY274
AALA280
AGLU348
ATYR362
AVAL366
AGLU377
AALA403

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P07953
ChainResidueDetails
AGLY359
APRO407

site_idSWS_FT_FI8
Number of Residues3
DetailsSITE: Transition state stabilizer => ECO:0000269|PubMed:22275052
ChainResidueDetails
AASP267
AGLY274
ASER402

222624

PDB entries from 2024-07-17

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