4FXF
Structure of M2 pyruvate kinase in complex with phenylalanine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003723 | molecular_function | RNA binding |
A | 0003729 | molecular_function | mRNA binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0004713 | molecular_function | protein tyrosine kinase activity |
A | 0004743 | molecular_function | pyruvate kinase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005791 | cellular_component | rough endoplasmic reticulum |
A | 0005829 | cellular_component | cytosol |
A | 0005929 | cellular_component | cilium |
A | 0006096 | biological_process | glycolytic process |
A | 0006417 | biological_process | regulation of translation |
A | 0012501 | biological_process | programmed cell death |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0023026 | molecular_function | MHC class II protein complex binding |
A | 0030955 | molecular_function | potassium ion binding |
A | 0031982 | cellular_component | vesicle |
A | 0032869 | biological_process | cellular response to insulin stimulus |
A | 0034774 | cellular_component | secretory granule lumen |
A | 0045296 | molecular_function | cadherin binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0061621 | biological_process | canonical glycolysis |
A | 0062023 | cellular_component | collagen-containing extracellular matrix |
A | 0070062 | cellular_component | extracellular exosome |
A | 1903561 | cellular_component | extracellular vesicle |
A | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
A | 2000767 | biological_process | positive regulation of cytoplasmic translation |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0003723 | molecular_function | RNA binding |
B | 0003729 | molecular_function | mRNA binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004713 | molecular_function | protein tyrosine kinase activity |
B | 0004743 | molecular_function | pyruvate kinase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005576 | cellular_component | extracellular region |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005791 | cellular_component | rough endoplasmic reticulum |
B | 0005829 | cellular_component | cytosol |
B | 0005929 | cellular_component | cilium |
B | 0006096 | biological_process | glycolytic process |
B | 0006417 | biological_process | regulation of translation |
B | 0012501 | biological_process | programmed cell death |
B | 0016301 | molecular_function | kinase activity |
B | 0016310 | biological_process | phosphorylation |
B | 0023026 | molecular_function | MHC class II protein complex binding |
B | 0030955 | molecular_function | potassium ion binding |
B | 0031982 | cellular_component | vesicle |
B | 0032869 | biological_process | cellular response to insulin stimulus |
B | 0034774 | cellular_component | secretory granule lumen |
B | 0045296 | molecular_function | cadherin binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0061621 | biological_process | canonical glycolysis |
B | 0062023 | cellular_component | collagen-containing extracellular matrix |
B | 0070062 | cellular_component | extracellular exosome |
B | 1903561 | cellular_component | extracellular vesicle |
B | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
B | 1904813 | cellular_component | ficolin-1-rich granule lumen |
B | 2000767 | biological_process | positive regulation of cytoplasmic translation |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0003723 | molecular_function | RNA binding |
C | 0003729 | molecular_function | mRNA binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0004713 | molecular_function | protein tyrosine kinase activity |
C | 0004743 | molecular_function | pyruvate kinase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005576 | cellular_component | extracellular region |
C | 0005634 | cellular_component | nucleus |
C | 0005737 | cellular_component | cytoplasm |
C | 0005739 | cellular_component | mitochondrion |
C | 0005791 | cellular_component | rough endoplasmic reticulum |
C | 0005829 | cellular_component | cytosol |
C | 0005929 | cellular_component | cilium |
C | 0006096 | biological_process | glycolytic process |
C | 0006417 | biological_process | regulation of translation |
C | 0012501 | biological_process | programmed cell death |
C | 0016301 | molecular_function | kinase activity |
C | 0016310 | biological_process | phosphorylation |
C | 0023026 | molecular_function | MHC class II protein complex binding |
C | 0030955 | molecular_function | potassium ion binding |
C | 0031982 | cellular_component | vesicle |
C | 0032869 | biological_process | cellular response to insulin stimulus |
C | 0034774 | cellular_component | secretory granule lumen |
C | 0045296 | molecular_function | cadherin binding |
C | 0046872 | molecular_function | metal ion binding |
C | 0061621 | biological_process | canonical glycolysis |
C | 0062023 | cellular_component | collagen-containing extracellular matrix |
C | 0070062 | cellular_component | extracellular exosome |
C | 1903561 | cellular_component | extracellular vesicle |
C | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
C | 1904813 | cellular_component | ficolin-1-rich granule lumen |
C | 2000767 | biological_process | positive regulation of cytoplasmic translation |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0003723 | molecular_function | RNA binding |
D | 0003729 | molecular_function | mRNA binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0004713 | molecular_function | protein tyrosine kinase activity |
D | 0004743 | molecular_function | pyruvate kinase activity |
D | 0005515 | molecular_function | protein binding |
D | 0005524 | molecular_function | ATP binding |
D | 0005576 | cellular_component | extracellular region |
D | 0005634 | cellular_component | nucleus |
D | 0005737 | cellular_component | cytoplasm |
D | 0005739 | cellular_component | mitochondrion |
D | 0005791 | cellular_component | rough endoplasmic reticulum |
D | 0005829 | cellular_component | cytosol |
D | 0005929 | cellular_component | cilium |
D | 0006096 | biological_process | glycolytic process |
D | 0006417 | biological_process | regulation of translation |
D | 0012501 | biological_process | programmed cell death |
D | 0016301 | molecular_function | kinase activity |
D | 0016310 | biological_process | phosphorylation |
D | 0023026 | molecular_function | MHC class II protein complex binding |
D | 0030955 | molecular_function | potassium ion binding |
D | 0031982 | cellular_component | vesicle |
D | 0032869 | biological_process | cellular response to insulin stimulus |
D | 0034774 | cellular_component | secretory granule lumen |
D | 0045296 | molecular_function | cadherin binding |
D | 0046872 | molecular_function | metal ion binding |
D | 0061621 | biological_process | canonical glycolysis |
D | 0062023 | cellular_component | collagen-containing extracellular matrix |
D | 0070062 | cellular_component | extracellular exosome |
D | 1903561 | cellular_component | extracellular vesicle |
D | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
D | 1904813 | cellular_component | ficolin-1-rich granule lumen |
D | 2000767 | biological_process | positive regulation of cytoplasmic translation |
Functional Information from PROSITE/UniProt
site_id | PS00110 |
Number of Residues | 13 |
Details | PYRUVATE_KINASE Pyruvate kinase active site signature. IkIISKIENhEGV |
Chain | Residue | Details |
A | ILE265-VAL277 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23064226 |
Chain | Residue | Details |
A | ASN70 | |
B | ASN70 | |
B | ARG106 | |
B | HIS464 | |
A | ARG106 | |
A | HIS464 | |
D | ASN70 | |
D | ARG106 | |
D | HIS464 | |
C | ASN70 | |
C | ARG106 | |
C | HIS464 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P30613 |
Chain | Residue | Details |
A | ARG73 | |
D | THR328 | |
C | ARG73 | |
C | LYS270 | |
C | GLY295 | |
C | ASP296 | |
C | THR328 | |
B | ARG73 | |
B | LYS270 | |
B | GLY295 | |
B | ASP296 | |
A | LYS270 | |
B | THR328 | |
A | GLY295 | |
A | ASP296 | |
A | THR328 | |
D | ARG73 | |
D | LYS270 | |
D | GLY295 | |
D | ASP296 |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF |
Chain | Residue | Details |
A | ASN75 | |
D | ASP113 | |
D | THR114 | |
D | ARG120 | |
D | LYS207 | |
D | GLU272 | |
C | ASN75 | |
C | SER77 | |
C | ASP113 | |
C | THR114 | |
C | ARG120 | |
A | SER77 | |
C | LYS207 | |
C | GLU272 | |
B | ASN75 | |
B | SER77 | |
B | ASP113 | |
B | THR114 | |
B | ARG120 | |
B | LYS207 | |
B | GLU272 | |
A | ASP113 | |
A | THR114 | |
A | ARG120 | |
A | LYS207 | |
A | GLU272 | |
D | ASN75 | |
D | SER77 |
site_id | SWS_FT_FI4 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF |
Chain | Residue | Details |
A | THR432 | |
C | TRP482 | |
C | ARG489 | |
C | ARG516 | |
B | THR432 | |
B | TRP482 | |
B | ARG489 | |
B | ARG516 | |
A | TRP482 | |
A | ARG489 | |
A | ARG516 | |
D | THR432 | |
D | TRP482 | |
D | ARG489 | |
D | ARG516 | |
C | THR432 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00549 |
Chain | Residue | Details |
A | LYS270 | |
D | LYS270 | |
C | LYS270 | |
B | LYS270 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | SITE: Crucial for phosphotyrosine binding => ECO:0000269|PubMed:27199445 |
Chain | Residue | Details |
A | LYS433 | |
D | LYS433 | |
C | LYS433 | |
B | LYS433 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: N-acetylserine => ECO:0000269|Ref.11, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712 |
Chain | Residue | Details |
A | SER2 | |
D | SER2 | |
C | SER2 | |
B | SER2 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: N6,N6,N6-trimethyllysine => ECO:0007744|PubMed:24129315 |
Chain | Residue | Details |
A | LYS3 | |
D | LYS3 | |
C | LYS3 | |
B | LYS3 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER37 | |
D | SER37 | |
C | SER37 | |
B | SER37 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | THR41 | |
D | THR41 | |
C | THR41 | |
B | THR41 |
site_id | SWS_FT_FI11 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS62 | |
A | LYS89 | |
D | LYS62 | |
D | LYS89 | |
C | LYS62 | |
C | LYS89 | |
B | LYS62 | |
B | LYS89 |
site_id | SWS_FT_FI12 |
Number of Residues | 8 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P52480 |
Chain | Residue | Details |
A | LYS66 | |
A | LYS498 | |
D | LYS66 | |
D | LYS498 | |
C | LYS66 | |
C | LYS498 | |
B | LYS66 | |
B | LYS498 |
site_id | SWS_FT_FI13 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11980 |
Chain | Residue | Details |
A | SER97 | |
A | SER100 | |
D | SER97 | |
D | SER100 | |
C | SER97 | |
C | SER100 | |
B | SER97 | |
B | SER100 |
site_id | SWS_FT_FI14 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | TYR105 | |
D | TYR105 | |
C | TYR105 | |
B | TYR105 |
site_id | SWS_FT_FI15 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER127 | |
D | SER127 | |
C | SER127 | |
B | SER127 |
site_id | SWS_FT_FI16 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P52480 |
Chain | Residue | Details |
A | TYR148 | |
D | TYR148 | |
C | TYR148 | |
B | TYR148 |
site_id | SWS_FT_FI17 |
Number of Residues | 8 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480 |
Chain | Residue | Details |
A | LYS166 | |
A | LYS322 | |
D | LYS166 | |
D | LYS322 | |
C | LYS166 | |
C | LYS322 | |
B | LYS166 | |
B | LYS322 |
site_id | SWS_FT_FI18 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
A | TYR175 | |
D | TYR175 | |
C | TYR175 | |
B | TYR175 |
site_id | SWS_FT_FI19 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
A | THR195 | |
D | THR195 | |
C | THR195 | |
B | THR195 |
site_id | SWS_FT_FI20 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS266 | |
D | LYS266 | |
C | LYS266 | |
B | LYS266 |
site_id | SWS_FT_FI21 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480 |
Chain | Residue | Details |
A | LYS270 | |
D | LYS270 | |
C | LYS270 | |
B | LYS270 |
site_id | SWS_FT_FI22 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:21700219 |
Chain | Residue | Details |
A | LYS305 | |
D | LYS305 | |
C | LYS305 | |
B | LYS305 |
site_id | SWS_FT_FI23 |
Number of Residues | 8 |
Details | MOD_RES: 4-hydroxyproline => ECO:0000269|PubMed:21620138 |
Chain | Residue | Details |
A | PRO403 | |
A | PRO408 | |
D | PRO403 | |
D | PRO408 | |
C | PRO403 | |
C | PRO408 | |
B | PRO403 | |
B | PRO408 |
site_id | SWS_FT_FI24 |
Number of Residues | 8 |
Details | MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:30487609 |
Chain | Residue | Details |
A | CYS423 | |
A | CYS424 | |
D | CYS423 | |
D | CYS424 | |
C | CYS423 | |
C | CYS424 | |
B | CYS423 | |
B | CYS424 |
site_id | SWS_FT_FI25 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:26787900, ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS433 | |
D | LYS433 | |
C | LYS433 | |
B | LYS433 |
site_id | SWS_FT_FI26 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P52480 |
Chain | Residue | Details |
A | LYS475 | |
D | LYS475 | |
C | LYS475 | |
B | LYS475 |
site_id | SWS_FT_FI27 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
A | LYS115 | |
D | LYS115 | |
C | LYS115 | |
B | LYS115 |
site_id | SWS_FT_FI28 |
Number of Residues | 12 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
B | LYS266 | |
B | LYS270 | |
A | LYS266 | |
A | LYS270 | |
D | LYS266 | |
D | LYS270 | |
C | LYS266 | |
C | LYS270 |
site_id | SWS_FT_FI29 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211 |
Chain | Residue | Details |
A | LYS166 | |
D | LYS166 | |
C | LYS166 | |
B | LYS166 |