Structure of PDB 4xyj Chain C

Receptor sequence
>4xyjC (length=760) Species: 9606 (Homo sapiens) [Search protein sequence]
RKFLEHLSGAGKAIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFIYEG
YQGMVDGGSNIAEADWESVSSILQVGGTIIGSARCQAFRTREGRLKAACN
LLQRGITNLCVIGGDGSLTGANLFRKEWSGLLEELARNGQIDKEAVQKYA
YLNVVGMVGSIDNDFCGTDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFV
LEVMGRHCGYLALVSALACGADWVFLPESPPEEGWEEQMCVKLSENRARK
KRLNIIIVAEGAIDTQNKPITSEKIKELVVTQLGYDTRVTILGHVQRGGT
PSAFDRILASRMGVEAVIALLEATPDTPACVVSLNGNHAVRLPLMECVQM
TQDVQKAMDERRFQDAVRLRGRSFAGNLNTYKRLAIKLPDDQIPKTNCNV
AVINVGAPAAGMNAAVRSAVRVGIADGHRMLAIYDGFDGFAKGQIKEIGW
TDVGGWTGQGGSILGTKRVLPGKYLEEIATQMRTHSINALLIIGGFEAYL
GLLELSAAREKHEEFCVPMVMVPATVSNNVPGSDFSIGADTALNTITDTC
DRIKQSASGTKRRVFIIETMGGYCGYLANMGGLAAGADAAYIFEEPFDIR
DLQSNVEHLTEKMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGKGVFD
CRKNVLGHMQQGGAPSPFDRNFGTKISARAMEWITAKLKEFTTDDSICVL
GISKRNVIFQPVAELKKQTDFEHRIPKEQWWLKLRPLMKILAKYKASYDV
SDSGQLEHVQ
3D structure
PDB4xyj Structures of human phosphofructokinase-1 and atomic basis of cancer-associated mutations.
ChainC
Resolution3.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G34 R97 C98 D128 G172 S173 D175 D177 R219
Catalytic site (residue number reindexed from 1) G21 R84 C85 D115 G159 S160 D162 D164 R206
Enzyme Commision number 2.7.1.11: 6-phosphofructokinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ATP C G33 G34 Y64 R97 C98 F101 R102 G127 D128 G129 S130 G133 S173 R219 G20 G21 Y51 R84 C85 F88 R89 G114 D115 G116 S117 G120 S160 R206
BS02 MG C G34 G126 G172 S173 G21 G113 G159 S160
BS03 PO4 C K264 R430 R434 G468 K251 R417 R421 G455
Gene Ontology
Molecular Function
GO:0003872 6-phosphofructokinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016208 AMP binding
GO:0016301 kinase activity
GO:0042802 identical protein binding
GO:0044877 protein-containing complex binding
GO:0045296 cadherin binding
GO:0046872 metal ion binding
GO:0048029 monosaccharide binding
GO:0070095 fructose-6-phosphate binding
Biological Process
GO:0006002 fructose 6-phosphate metabolic process
GO:0006096 glycolytic process
GO:0016310 phosphorylation
GO:0030388 fructose 1,6-bisphosphate metabolic process
GO:0061621 canonical glycolysis
GO:1990830 cellular response to leukemia inhibitory factor
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005945 6-phosphofructokinase complex
GO:0016020 membrane
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4xyj, PDBe:4xyj, PDBj:4xyj
PDBsum4xyj
PubMed25985179
UniProtQ01813|PFKAP_HUMAN ATP-dependent 6-phosphofructokinase, platelet type (Gene Name=PFKP)

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