3BV4
Crystal structure of a rabbit muscle fructose-1,6-bisphosphate aldolase A dimer variant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0030335 | biological_process | positive regulation of cell migration |
| A | 0031430 | cellular_component | M band |
| A | 0031674 | cellular_component | I band |
| A | 0034316 | biological_process | negative regulation of Arp2/3 complex-mediated actin nucleation |
| A | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1 |
| Chain | Residue |
| A | LYS41 |
| A | ARG42 |
| A | ARG303 |
| A | HOH3671 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2 |
| Chain | Residue |
| A | THR51 |
| A | GLU52 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3 |
| Chain | Residue |
| A | ARG258 |
| A | LYS12 |
| A | LYS199 |
| A | GLN202 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 345 |
| Chain | Residue |
| A | HIS80 |
| A | LYS110 |
| A | HOH3457 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 346 |
| Chain | Residue |
| A | SER275 |
| A | HOH3458 |
| A | HOH3696 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 347 |
| Chain | Residue |
| A | ASP66 |
| A | ASP67 |
| A | LYS311 |
| A | HOH3451 |
| A | HOH3598 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 13P A 3371 |
| Chain | Residue |
| A | LYS229 |
| A | LEU270 |
| A | SER271 |
| A | GLY272 |
| A | SER300 |
| A | TYR301 |
| A | GLY302 |
| A | ARG303 |
| A | HOH3655 |
| A | HOH3657 |
| A | HOH3659 |
| A | HOH3661 |
| A | HOH3667 |
Functional Information from PROSITE/UniProt
| site_id | PS00158 |
| Number of Residues | 11 |
| Details | ALDOLASE_CLASS_I Fructose-bisphosphate aldolase class-I active site. IyLEGtLLKPN |
| Chain | Residue | Details |
| A | ILE221-ASN231 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:11779856 |
| Chain | Residue | Details |
| A | GLU187 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Schiff-base intermediate with dihydroxyacetone-P => ECO:0000269|PubMed:11779856 |
| Chain | Residue | Details |
| A | LYS229 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD |
| Chain | Residue | Details |
| A | ARG42 | |
| A | SER271 | |
| A | SER300 | |
| A | ARG303 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Essential for substrate cleavage |
| Chain | Residue | Details |
| A | CYS72 | |
| A | LYS107 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | SITE: Alkylation inactivates the enzyme |
| Chain | Residue | Details |
| A | LYS146 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04075 |
| Chain | Residue | Details |
| A | THR8 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04075 |
| Chain | Residue | Details |
| A | SER35 | |
| A | SER38 | |
| A | SER45 | |
| A | SER271 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P04075 |
| Chain | Residue | Details |
| A | LYS41 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 |
| Chain | Residue | Details |
| A | LYS98 | |
| A | LYS146 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P04075 |
| Chain | Residue | Details |
| A | LYS107 | |
| A | LYS329 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-malonyllysine; alternate => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS110 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P05065 |
| Chain | Residue | Details |
| A | SER131 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-malonyllysine => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS311 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P04075 |
| Chain | Residue | Details |
| A | LYS41 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ald |
| Chain | Residue | Details |
| A | GLU187 | |
| A | LYS229 | |
| A | ASP33 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 222 |
| Chain | Residue | Details |
| A | ASP33 | electrostatic stabiliser, hydrogen bond acceptor |
| A | LYS146 | electrostatic stabiliser, hydrogen bond donor |
| A | GLU187 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, proton relay |
| A | GLU189 | activator, electrostatic stabiliser, hydrogen bond acceptor, polar interaction |
| A | LYS229 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor, proton relay |
| A | SER300 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
