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

4OMT

Crystal structure of human muscle phosphofructokinase (dissociated homodimer)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0003872molecular_function6-phosphofructokinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005945cellular_component6-phosphofructokinase complex
A0005980biological_processglycogen catabolic process
A0006002biological_processfructose 6-phosphate metabolic process
A0006096biological_processglycolytic process
A0008443molecular_functionphosphofructokinase activity
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016324cellular_componentapical plasma membrane
A0016740molecular_functiontransferase activity
A0019900molecular_functionkinase binding
A0030388biological_processfructose 1,6-bisphosphate metabolic process
A0032024biological_processpositive regulation of insulin secretion
A0042593biological_processglucose homeostasis
A0042802molecular_functionidentical protein binding
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046716biological_processmuscle cell cellular homeostasis
A0046835biological_processcarbohydrate phosphorylation
A0046872molecular_functionmetal ion binding
A0061615biological_processglycolytic process through fructose-6-phosphate
A0061621biological_processcanonical glycolysis
A0070061molecular_functionfructose binding
A0070095molecular_functionfructose-6-phosphate binding
A0093001biological_processglycolysis from storage polysaccharide through glucose-1-phosphate
A0097228cellular_componentsperm principal piece
Functional Information from PROSITE/UniProt
site_idPS00433
Number of Residues19
DetailsPHOSPHOFRUCTOKINASE Phosphofructokinase signature. RvtvlGHvQRGGtpsafDR
ChainResidueDetails
AARG292-ARG310
AARG655-ARG673

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsRegion: {"description":"Interdomain linker"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_03184","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03184","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_03184","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P47858","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P47857","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"29775581","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

PDB statisticsPDBj update infoContact PDBjnumon