5OHG
enolase in complex with RNase E
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000015 | cellular_component | phosphopyruvate hydratase complex |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004634 | molecular_function | phosphopyruvate hydratase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0006096 | biological_process | glycolytic process |
| A | 0006396 | biological_process | RNA processing |
| A | 0006401 | biological_process | RNA catabolic process |
| A | 0009986 | cellular_component | cell surface |
| A | 0016020 | cellular_component | membrane |
| A | 0016829 | molecular_function | lyase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1990061 | cellular_component | bacterial degradosome |
| B | 0000015 | cellular_component | phosphopyruvate hydratase complex |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004634 | molecular_function | phosphopyruvate hydratase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005856 | cellular_component | cytoskeleton |
| B | 0006096 | biological_process | glycolytic process |
| B | 0006396 | biological_process | RNA processing |
| B | 0006401 | biological_process | RNA catabolic process |
| B | 0009986 | cellular_component | cell surface |
| B | 0016020 | cellular_component | membrane |
| B | 0016829 | molecular_function | lyase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 1990061 | cellular_component | bacterial degradosome |
| H | 0000015 | cellular_component | phosphopyruvate hydratase complex |
| H | 0000287 | molecular_function | magnesium ion binding |
| H | 0004634 | molecular_function | phosphopyruvate hydratase activity |
| H | 0005515 | molecular_function | protein binding |
| H | 0005576 | cellular_component | extracellular region |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0005829 | cellular_component | cytosol |
| H | 0005856 | cellular_component | cytoskeleton |
| H | 0006096 | biological_process | glycolytic process |
| H | 0006396 | biological_process | RNA processing |
| H | 0006401 | biological_process | RNA catabolic process |
| H | 0009986 | cellular_component | cell surface |
| H | 0016020 | cellular_component | membrane |
| H | 0016829 | molecular_function | lyase activity |
| H | 0042802 | molecular_function | identical protein binding |
| H | 0042803 | molecular_function | protein homodimerization activity |
| H | 0046872 | molecular_function | metal ion binding |
| H | 1990061 | cellular_component | bacterial degradosome |
| I | 0000015 | cellular_component | phosphopyruvate hydratase complex |
| I | 0000287 | molecular_function | magnesium ion binding |
| I | 0004634 | molecular_function | phosphopyruvate hydratase activity |
| I | 0005515 | molecular_function | protein binding |
| I | 0005576 | cellular_component | extracellular region |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0005829 | cellular_component | cytosol |
| I | 0005856 | cellular_component | cytoskeleton |
| I | 0006096 | biological_process | glycolytic process |
| I | 0006396 | biological_process | RNA processing |
| I | 0006401 | biological_process | RNA catabolic process |
| I | 0009986 | cellular_component | cell surface |
| I | 0016020 | cellular_component | membrane |
| I | 0016829 | molecular_function | lyase activity |
| I | 0042802 | molecular_function | identical protein binding |
| I | 0042803 | molecular_function | protein homodimerization activity |
| I | 0046872 | molecular_function | metal ion binding |
| I | 1990061 | cellular_component | bacterial degradosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 501 |
| Chain | Residue |
| A | ASP246 |
| A | GLU290 |
| A | ASP317 |
| A | LYS342 |
| A | HOH611 |
| A | HOH632 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 502 |
| Chain | Residue |
| A | ASN162 |
| A | VAL164 |
| A | HOH918 |
| A | GLY156 |
| A | GLY157 |
| A | ALA160 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 A 503 |
| Chain | Residue |
| A | GLY40 |
| A | ALA41 |
| A | SER42 |
| A | HIS159 |
| A | GLN167 |
| A | LYS342 |
| A | ARG371 |
| A | SER372 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 501 |
| Chain | Residue |
| B | ASP246 |
| B | GLU290 |
| B | ASP317 |
| B | HOH616 |
| B | HOH619 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 502 |
| Chain | Residue |
| B | GLY156 |
| B | GLY157 |
| B | ALA160 |
| B | ASN162 |
| B | VAL164 |
| B | HOH873 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 B 503 |
| Chain | Residue |
| B | GLY40 |
| B | ALA41 |
| B | SER42 |
| B | HIS159 |
| B | GLN167 |
| B | LYS342 |
| B | ARG371 |
| B | SER372 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue MG H 501 |
| Chain | Residue |
| H | ASP246 |
| H | GLU290 |
| H | ASP317 |
| H | LYS342 |
| H | HOH603 |
| H | HOH673 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue NA H 502 |
| Chain | Residue |
| H | GLY157 |
| H | ALA160 |
| H | ASN162 |
| H | VAL164 |
| H | HOH927 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 H 503 |
| Chain | Residue |
| H | GLY40 |
| H | ALA41 |
| H | SER42 |
| H | HIS159 |
| H | GLN167 |
| H | LYS342 |
| H | ARG371 |
| H | SER372 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue MG I 501 |
| Chain | Residue |
| I | ASP246 |
| I | GLU290 |
| I | ASP317 |
| I | LYS342 |
| I | HOH616 |
| I | HOH621 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue NA I 502 |
| Chain | Residue |
| I | ASP53 |
| I | ASP55 |
| I | ARG58 |
| I | GLY61 |
| I | LYS62 |
| I | GLY63 |
| I | HOH701 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue NA I 503 |
| Chain | Residue |
| I | GLY157 |
| I | ALA160 |
| I | ASN162 |
| I | VAL164 |
| I | HOH873 |
| site_id | AD4 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 I 504 |
| Chain | Residue |
| I | GLY40 |
| I | ALA41 |
| I | SER42 |
| I | HIS159 |
| I | GLN167 |
| I | LYS342 |
| I | ARG371 |
| I | SER372 |
Functional Information from PROSITE/UniProt
| site_id | PS00164 |
| Number of Residues | 14 |
| Details | ENOLASE Enolase signature. ILIKfNQIGSLTET |
| Chain | Residue | Details |
| A | ILE339-THR352 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:15003462 |
| Chain | Residue | Details |
| A | GLU209 | |
| B | GLU209 | |
| H | GLU209 | |
| I | GLU209 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:15003462 |
| Chain | Residue | Details |
| A | LYS342 | |
| B | LYS342 | |
| H | LYS342 | |
| I | LYS342 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0007744|PDB:6BFZ |
| Chain | Residue | Details |
| A | ALA41 | |
| B | SER372 | |
| H | ALA41 | |
| H | GLN167 | |
| H | LYS342 | |
| H | ARG371 | |
| H | SER372 | |
| I | ALA41 | |
| I | GLN167 | |
| I | LYS342 | |
| I | ARG371 | |
| A | GLN167 | |
| I | SER372 | |
| A | LYS342 | |
| A | ARG371 | |
| A | SER372 | |
| B | ALA41 | |
| B | GLN167 | |
| B | LYS342 | |
| B | ARG371 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30714720, ECO:0007744|PDB:6BFY |
| Chain | Residue | Details |
| A | SER42 | |
| B | SER42 | |
| H | SER42 | |
| I | SER42 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0007744|PDB:6BFY |
| Chain | Residue | Details |
| A | HIS159 | |
| A | GLU209 | |
| B | HIS159 | |
| B | GLU209 | |
| H | HIS159 | |
| H | GLU209 | |
| I | HIS159 | |
| I | GLU209 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0007744|PDB:6BFY, ECO:0007744|PDB:6BFZ |
| Chain | Residue | Details |
| A | GLU168 | |
| B | GLU168 | |
| H | GLU168 | |
| I | GLU168 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:11676541, ECO:0000269|PubMed:16516921, ECO:0000269|PubMed:20823555, ECO:0007744|PDB:1E9I, ECO:0007744|PDB:2FYM, ECO:0007744|PDB:3H8A, ECO:0007744|PDB:6BFY, ECO:0007744|PDB:6BFZ |
| Chain | Residue | Details |
| A | ASP246 | |
| B | ASP246 | |
| H | ASP246 | |
| I | ASP246 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:11676541, ECO:0000269|PubMed:20823555, ECO:0000269|PubMed:30714720, ECO:0007744|PDB:1E9I, ECO:0007744|PDB:2FYM, ECO:0007744|PDB:3H8A, ECO:0007744|PDB:6BFY, ECO:0007744|PDB:6BFZ |
| Chain | Residue | Details |
| A | GLU290 | |
| B | GLU290 | |
| H | GLU290 | |
| I | GLU290 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:11676541, ECO:0000269|PubMed:16516921, ECO:0000269|PubMed:20823555, ECO:0007744|PDB:1E9I, ECO:0007744|PDB:2FYM, ECO:0007744|PDB:6BFY, ECO:0007744|PDB:6BFZ |
| Chain | Residue | Details |
| A | ASP317 | |
| B | ASP317 | |
| H | ASP317 | |
| I | ASP317 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0007744|PDB:6BFY, ECO:0007744|PDB:6BFZ |
| Chain | Residue | Details |
| A | LYS393 | |
| B | LYS393 | |
| H | LYS393 | |
| I | LYS393 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 12 |
| Details | SITE: Interaction with RNase E => ECO:0000269|PubMed:16516921, ECO:0000269|PubMed:20823555 |
| Chain | Residue | Details |
| A | LYS120 | |
| I | LYS120 | |
| I | GLU376 | |
| I | GLN408 | |
| A | GLU376 | |
| A | GLN408 | |
| B | LYS120 | |
| B | GLU376 | |
| B | GLN408 | |
| H | LYS120 | |
| H | GLU376 | |
| H | GLN408 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | LYS257 | |
| B | LYS257 | |
| H | LYS257 | |
| I | LYS257 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:31328167 |
| Chain | Residue | Details |
| A | LYS342 | |
| B | LYS342 | |
| H | LYS342 | |
| I | LYS342 |
