Structure of PDB 4xyk Chain A

Receptor sequence
>4xykA (length=737) Species: 9606 (Homo sapiens) [Search protein sequence]
LEHLSGAGKAIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFIYEGYQG
MVDGGSNIAEADWESVSSILQVGGTIIGSARCQAFRTREGRLKAACNLLQ
RGITNLCVIGGDGSLTGANLFRKEWSGLLEELARNGQIDKEAVQKYAYLN
VVGMVGSIDNDFCGTDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEV
MGRHCGYLALVSALACGADWVFLPESPPEEGWEEQMCVKLSENRARKKRL
NIIIVAEGAIDTQNKPITSEKIKELVVTQLGYDTRVTILGHVQRGGTPSA
FDRILASRMGVEAVIALLEATPDTPACVVSLNGNHAVRLPLMECVQMTQD
VQKAMDERRFQDAVRLRGRSFAGNLNTYKRLAIKLPDDQIPKTNCNVAVI
NVGAPAAGMNAAVRSAVRVGIADGHRMLAIYDGFDGFAKGQIKEIGWTDV
GGWTGQGGSILGTKRVLPGKYLEEIATQMRTHSINALLIIGGFEAYLGLL
ELSAAREKHEEFCVPMVMVPATVSNNVPGSDFSIGADTALNTITDTCDRI
KQKRRVFIIETMGGYCGYLANMGGLAAGADAAYIFEEPFDIRDLQSNVEH
LTEKMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGKGVFDCRKNVLGH
MQQGGAPSPFDRNFGTKISARAMEWITAKLKEAKFTTDDSICVLGISKRN
VIFQPVAELKKQTDFEHRIPKEQWWLKLRPLMKILAK
3D structure
PDB4xyk Structures of human phosphofructokinase-1 and atomic basis of cancer-associated mutations.
ChainA
Resolution3.4 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) G18 R81 C82 D112 G156 S157 D159 D161 R203
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 ADP A Y64 R97 C98 R102 G127 D128 G129 S130 Y48 R81 C82 R86 G111 D112 G113 S114
BS02 PO4 A K264 R430 R434 G467 G468 K248 R414 R418 G451 G452
BS03 PO4 A R44 R48 S83 R28 R32 S67
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:4xyk, PDBe:4xyk, PDBj:4xyk
PDBsum4xyk
PubMed25985179
UniProtQ01813|PFKAP_HUMAN ATP-dependent 6-phosphofructokinase, platelet type (Gene Name=PFKP)

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