3UJF
Asymmetric complex of human neuron specific enolase-4-PGA/PEP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000015 | cellular_component | phosphopyruvate hydratase complex |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0001917 | cellular_component | photoreceptor inner segment |
A | 0004634 | molecular_function | phosphopyruvate hydratase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005615 | cellular_component | extracellular space |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0005938 | cellular_component | cell cortex |
A | 0006094 | biological_process | gluconeogenesis |
A | 0006096 | biological_process | glycolytic process |
A | 0009410 | biological_process | response to xenobiotic stimulus |
A | 0009986 | cellular_component | cell surface |
A | 0016020 | cellular_component | membrane |
A | 0016829 | molecular_function | lyase activity |
A | 0019899 | molecular_function | enzyme binding |
A | 0030426 | cellular_component | growth cone |
A | 0032355 | biological_process | response to estradiol |
A | 0042802 | molecular_function | identical protein binding |
A | 0043025 | cellular_component | neuronal cell body |
A | 0043204 | cellular_component | perikaryon |
A | 0044877 | molecular_function | protein-containing complex binding |
A | 0045121 | cellular_component | membrane raft |
A | 0046872 | molecular_function | metal ion binding |
A | 0061621 | biological_process | canonical glycolysis |
A | 0070062 | cellular_component | extracellular exosome |
A | 0097060 | cellular_component | synaptic membrane |
B | 0000015 | cellular_component | phosphopyruvate hydratase complex |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0001917 | cellular_component | photoreceptor inner segment |
B | 0004634 | molecular_function | phosphopyruvate hydratase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005615 | cellular_component | extracellular space |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
B | 0005938 | cellular_component | cell cortex |
B | 0006094 | biological_process | gluconeogenesis |
B | 0006096 | biological_process | glycolytic process |
B | 0009410 | biological_process | response to xenobiotic stimulus |
B | 0009986 | cellular_component | cell surface |
B | 0016020 | cellular_component | membrane |
B | 0016829 | molecular_function | lyase activity |
B | 0019899 | molecular_function | enzyme binding |
B | 0030426 | cellular_component | growth cone |
B | 0032355 | biological_process | response to estradiol |
B | 0042802 | molecular_function | identical protein binding |
B | 0043025 | cellular_component | neuronal cell body |
B | 0043204 | cellular_component | perikaryon |
B | 0044877 | molecular_function | protein-containing complex binding |
B | 0045121 | cellular_component | membrane raft |
B | 0046872 | molecular_function | metal ion binding |
B | 0061621 | biological_process | canonical glycolysis |
B | 0070062 | cellular_component | extracellular exosome |
B | 0097060 | cellular_component | synaptic membrane |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 501 |
Chain | Residue |
A | ASP244 |
A | GLU292 |
A | ASP317 |
A | LYS393 |
A | 2PG503 |
A | HOH601 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 502 |
Chain | Residue |
A | HOH603 |
A | SER39 |
A | 2PG503 |
A | HOH602 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE 2PG A 503 |
Chain | Residue |
A | GLY37 |
A | ALA38 |
A | SER39 |
A | HIS157 |
A | GLN165 |
A | GLU166 |
A | GLU209 |
A | ASP244 |
A | GLU292 |
A | ASP317 |
A | LYS342 |
A | HIS370 |
A | ARG371 |
A | SER372 |
A | LYS393 |
A | MG501 |
A | MG502 |
A | HOH602 |
A | HOH603 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 501 |
Chain | Residue |
B | ASP244 |
B | GLU292 |
B | ASP317 |
B | PEP503 |
B | HOH601 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B 502 |
Chain | Residue |
B | SER39 |
B | PEP503 |
B | HOH602 |
B | HOH603 |
site_id | AC6 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE PEP B 503 |
Chain | Residue |
B | GLY37 |
B | ALA38 |
B | SER39 |
B | GLN165 |
B | GLU166 |
B | GLU209 |
B | ASP244 |
B | GLU292 |
B | ASP317 |
B | LYS342 |
B | HIS370 |
B | ARG371 |
B | SER372 |
B | LYS393 |
B | MG501 |
B | MG502 |
B | HOH603 |
Functional Information from PROSITE/UniProt
site_id | PS00164 |
Number of Residues | 14 |
Details | ENOLASE Enolase signature. LLLKvNQIGSVTEA |
Chain | Residue | Details |
A | LEU339-ALA352 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P00924 |
Chain | Residue | Details |
A | GLU209 | |
B | GLU209 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P00924 |
Chain | Residue | Details |
A | LYS342 | |
B | LYS342 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P06733 |
Chain | Residue | Details |
A | SER39 | |
B | SER39 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00924 |
Chain | Residue | Details |
A | HIS157 | |
B | ASP317 | |
B | SER369 | |
B | LYS393 | |
A | GLU166 | |
A | GLU292 | |
A | ASP317 | |
A | SER369 | |
A | LYS393 | |
B | HIS157 | |
B | GLU166 | |
B | GLU292 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP244 | |
B | ASP244 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P06733 |
Chain | Residue | Details |
A | SER1 | |
B | SER1 |
site_id | SWS_FT_FI7 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P06733 |
Chain | Residue | Details |
A | LYS4 | |
A | LYS63 | |
A | LYS192 | |
A | LYS255 | |
B | LYS4 | |
B | LYS63 | |
B | LYS192 | |
B | LYS255 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
A | THR25 | |
B | THR25 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455 |
Chain | Residue | Details |
A | TYR43 | |
B | TYR43 |
site_id | SWS_FT_FI10 |
Number of Residues | 6 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 |
Chain | Residue | Details |
A | LYS59 | |
A | LYS88 | |
A | LYS227 | |
B | LYS59 | |
B | LYS88 | |
B | LYS227 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P17183 |
Chain | Residue | Details |
A | LYS196 | |
A | LYS198 | |
B | LYS196 | |
B | LYS198 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P17182 |
Chain | Residue | Details |
A | LYS201 | |
B | LYS201 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P06733 |
Chain | Residue | Details |
A | LYS232 | |
B | LYS232 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER262 | |
B | SER262 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06733 |
Chain | Residue | Details |
A | TYR286 | |
B | TYR286 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06733 |
Chain | Residue | Details |
A | SER290 | |
B | SER290 |
site_id | SWS_FT_FI17 |
Number of Residues | 6 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P17182 |
Chain | Residue | Details |
A | LYS334 | |
A | LYS342 | |
A | LYS405 | |
B | LYS334 | |
B | LYS342 | |
B | LYS405 |
site_id | SWS_FT_FI18 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P06733 |
Chain | Residue | Details |
A | LYS201 | |
B | LYS201 |