1PKN
STRUCTURE OF RABBIT MUSCLE PYRUVATE KINASE COMPLEXED WITH MN2+, K+, AND PYRUVATE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion 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 | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005791 | cellular_component | rough endoplasmic reticulum |
| A | 0006096 | biological_process | glycolytic process |
| A | 0006417 | biological_process | regulation of translation |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0030955 | molecular_function | potassium ion binding |
| A | 0032869 | biological_process | cellular response to insulin stimulus |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| A | 2000767 | biological_process | positive regulation of cytoplasmic translation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K A 532 |
| Chain | Residue |
| A | ASN74 |
| A | SER76 |
| A | ASP112 |
| A | THR113 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN A 534 |
| Chain | Residue |
| A | GLU271 |
| A | ASP295 |
| A | PYR533 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PYR A 533 |
| Chain | Residue |
| A | MET290 |
| A | ALA292 |
| A | GLY294 |
| A | ASP295 |
| A | THR327 |
| A | MN534 |
| A | LYS269 |
| A | GLU271 |
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 | ILE264-VAL276 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P14618 |
| Chain | Residue | Details |
| A | VAL70 | |
| A | GLU432 | |
| A | LEU464 | |
| A | ALA482 | |
| A | VAL489 | |
| A | PRO516 | |
| A | PHE75 | |
| A | HIS77 | |
| A | PRO106 | |
| A | THR113 | |
| A | LYS114 | |
| A | THR120 | |
| A | GLY207 | |
| A | ASN272 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P30613 |
| Chain | Residue | Details |
| A | MET73 | |
| A | ILE270 | |
| A | ASP295 | |
| A | LEU296 | |
| A | GLN328 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00549 |
| Chain | Residue | Details |
| A | ILE270 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P11979 |
| Chain | Residue | Details |
| A | LYS2 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N6,N6,N6-trimethyllysine => ECO:0000250|UniProtKB:P14618 |
| Chain | Residue | Details |
| A | SER3 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P14618 |
| Chain | Residue | Details |
| A | ALA37 | |
| A | GLY127 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P14618 |
| Chain | Residue | Details |
| A | ALA41 | |
| A | GLU195 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P14618 |
| Chain | Residue | Details |
| A | GLU62 | |
| A | ASN89 | |
| A | VAL305 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P52480 |
| Chain | Residue | Details |
| A | SER66 | |
| A | ALA498 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11980 |
| Chain | Residue | Details |
| A | PHE97 | |
| A | ASP100 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P14618 |
| Chain | Residue | Details |
| A | ARG105 | |
| A | VAL175 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P52480 |
| Chain | Residue | Details |
| A | MET148 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480 |
| Chain | Residue | Details |
| A | VAL166 | |
| A | PRO322 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P14618 |
| Chain | Residue | Details |
| A | ILE266 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480 |
| Chain | Residue | Details |
| A | ILE270 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P52480 |
| Chain | Residue | Details |
| A | ASP475 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 1 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P14618 |
| Chain | Residue | Details |
| A | GLY115 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 3 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P14618 |
| Chain | Residue | Details |
| A | ILE266 | |
| A | ILE270 |
| site_id | SWS_FT_FI19 |
| Number of Residues | 1 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0000250|UniProtKB:P14618 |
| Chain | Residue | Details |
| A | VAL166 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 8193145 |
| Chain | Residue | Details |
| A | LYS269 | |
| A | SER361 | |
| A | ARG119 | |
| A | GLU363 | |
| A | ARG72 | |
| A | THR327 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| A | MET73 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| A | THR120 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| A | ILE270 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| A | GLN328 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
