4ALD
HUMAN MUSCLE FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE COMPLEXED WITH FRUCTOSE 1,6-BISPHOSPHATE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003779 | molecular_function | actin binding |
| A | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006000 | biological_process | fructose metabolic process |
| A | 0006096 | biological_process | glycolytic process |
| A | 0006754 | biological_process | ATP biosynthetic process |
| A | 0006941 | biological_process | striated muscle contraction |
| A | 0007015 | biological_process | actin filament organization |
| A | 0007339 | biological_process | binding of sperm to zona pellucida |
| A | 0008092 | molecular_function | cytoskeletal protein binding |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0015629 | cellular_component | actin cytoskeleton |
| A | 0015631 | molecular_function | tubulin binding |
| A | 0016020 | cellular_component | membrane |
| A | 0016829 | molecular_function | lyase activity |
| A | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
| A | 0031093 | cellular_component | platelet alpha granule lumen |
| A | 0031430 | cellular_component | M band |
| A | 0031674 | cellular_component | I band |
| A | 0034774 | cellular_component | secretory granule lumen |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0045296 | molecular_function | cadherin binding |
| A | 0046716 | biological_process | muscle cell cellular homeostasis |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 0061827 | cellular_component | sperm head |
| A | 0070061 | molecular_function | fructose binding |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 1904724 | cellular_component | tertiary granule lumen |
| A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE 2FP A 364 |
| Chain | Residue |
| A | GLU187 |
| A | LYS229 |
| A | LEU270 |
| A | SER271 |
| A | GLY272 |
| A | SER300 |
| A | TYR301 |
| A | GLY302 |
| A | ARG303 |
| A | ALA304 |
| A | ALA31 |
| A | ASP33 |
| A | GLU34 |
| A | SER35 |
| A | SER38 |
| A | LYS107 |
| A | LYS146 |
| A | ARG148 |
| site_id | SBL |
| Number of Residues | 1 |
| Details | SCHIFF'S BASE LYSINE |
| Chain | Residue |
| A | LYS229 |
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:0000250|UniProtKB:P00883 |
| Chain | Residue | Details |
| A | PRO188 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Schiff-base intermediate with dihydroxyacetone-P => ECO:0000250|UniProtKB:P00883 |
| Chain | Residue | Details |
| A | PRO230 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00883 |
| Chain | Residue | Details |
| A | LEU43 | |
| A | GLY272 | |
| A | TYR301 | |
| A | ALA304 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P05065 |
| Chain | Residue | Details |
| A | PRO5 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | PRO9 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | THR36 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | ILE39 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | ARG42 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | ILE46 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29775581 |
| Chain | Residue | Details |
| A | SER99 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | VAL108 | |
| A | ARG330 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 |
| Chain | Residue | Details |
| A | GLY111 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P05065 |
| Chain | Residue | Details |
| A | GLU132 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674 |
| Chain | Residue | Details |
| A | TRP147 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | GLY272 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-malonyllysine => ECO:0000269|PubMed:21908771 |
| Chain | Residue | Details |
| A | ALA312 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25114211 |
| Chain | Residue | Details |
| A | ARG42 |
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 |
