7CLL
Mycobacterium tubeculosis enolase in complex with 2-Phosphoglycerate
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 | 0005576 | cellular_component | extracellular region |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006096 | biological_process | glycolytic process |
| A | 0009274 | cellular_component | peptidoglycan-based cell wall |
| A | 0009986 | cellular_component | cell surface |
| A | 0016829 | molecular_function | lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000015 | cellular_component | phosphopyruvate hydratase complex |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004634 | molecular_function | phosphopyruvate hydratase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006096 | biological_process | glycolytic process |
| B | 0009274 | cellular_component | peptidoglycan-based cell wall |
| B | 0009986 | cellular_component | cell surface |
| B | 0016829 | molecular_function | lyase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000015 | cellular_component | phosphopyruvate hydratase complex |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004634 | molecular_function | phosphopyruvate hydratase activity |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006096 | biological_process | glycolytic process |
| C | 0009274 | cellular_component | peptidoglycan-based cell wall |
| C | 0009986 | cellular_component | cell surface |
| C | 0016829 | molecular_function | lyase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000015 | cellular_component | phosphopyruvate hydratase complex |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004634 | molecular_function | phosphopyruvate hydratase activity |
| D | 0005576 | cellular_component | extracellular region |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006096 | biological_process | glycolytic process |
| D | 0009274 | cellular_component | peptidoglycan-based cell wall |
| D | 0009986 | cellular_component | cell surface |
| D | 0016829 | molecular_function | lyase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00164 |
| Number of Residues | 14 |
| Details | ENOLASE Enolase signature. LLVKvNQIGTLTET |
| Chain | Residue | Details |
| A | LEU332-THR345 |
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:0000305|PubMed:37860976 |
| Chain | Residue | Details |
| A | GLU204 | |
| B | GLU204 | |
| C | GLU204 | |
| D | GLU204 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000305|PubMed:37860976 |
| Chain | Residue | Details |
| A | LYS335 | |
| B | LYS335 | |
| C | LYS335 | |
| D | LYS335 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:37860976, ECO:0007744|PDB:6L7D, ECO:0007744|PDB:7CLK, ECO:0007744|PDB:7CLL |
| Chain | Residue | Details |
| A | ALA41 | |
| B | ALA41 | |
| C | ALA41 | |
| D | ALA41 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:37860976, ECO:0007744|PDB:7E4F |
| Chain | Residue | Details |
| C | SER42 | |
| C | GLN162 | |
| D | SER42 | |
| D | GLN162 | |
| A | SER42 | |
| A | GLN162 | |
| B | SER42 | |
| B | GLN162 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:37860976, ECO:0007744|PDB:7CLL |
| Chain | Residue | Details |
| A | GLU163 | |
| A | GLU204 | |
| B | GLU163 | |
| B | GLU204 | |
| C | GLU163 | |
| C | GLU204 | |
| D | GLU163 | |
| D | GLU204 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:37860976, ECO:0007744|PDB:6L7D, ECO:0007744|PDB:7CKP, ECO:0007744|PDB:7CLK, ECO:0007744|PDB:7CLL, ECO:0007744|PDB:7DLR, ECO:0007744|PDB:7E4F |
| Chain | Residue | Details |
| A | ASP241 | |
| A | ASP310 | |
| B | ASP241 | |
| B | ASP310 | |
| C | ASP241 | |
| C | ASP310 | |
| D | ASP241 | |
| D | ASP310 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:37860976, ECO:0007744|PDB:7CKP |
| Chain | Residue | Details |
| A | GLU283 | |
| B | GLU283 | |
| C | GLU283 | |
| D | GLU283 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:37860976, ECO:0007744|PDB:7CLK |
| Chain | Residue | Details |
| A | ASP311 | |
| B | ASP311 | |
| C | ASP311 | |
| D | ASP311 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:37860976, ECO:0007744|PDB:7DLR, ECO:0007744|PDB:7E4F |
| Chain | Residue | Details |
| A | LYS335 | |
| C | ARG364 | |
| C | SER365 | |
| C | LYS386 | |
| D | LYS335 | |
| D | ARG364 | |
| D | SER365 | |
| D | LYS386 | |
| A | ARG364 | |
| A | SER365 | |
| A | LYS386 | |
| B | LYS335 | |
| B | ARG364 | |
| B | SER365 | |
| B | LYS386 | |
| C | LYS335 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 44 |
| Details | MOD_RES: Glutamate methyl ester (Glu) => ECO:0000305|PubMed:37385399 |
| Chain | Residue | Details |
| A | GLU45 | |
| A | GLU406 | |
| A | GLU407 | |
| B | GLU45 | |
| B | GLU47 | |
| B | GLU50 | |
| B | GLU73 | |
| B | GLU126 | |
| B | GLU195 | |
| B | GLU204 | |
| B | GLU367 | |
| A | GLU47 | |
| B | GLU369 | |
| B | GLU406 | |
| B | GLU407 | |
| C | GLU45 | |
| C | GLU47 | |
| C | GLU50 | |
| C | GLU73 | |
| C | GLU126 | |
| C | GLU195 | |
| C | GLU204 | |
| A | GLU50 | |
| C | GLU367 | |
| C | GLU369 | |
| C | GLU406 | |
| C | GLU407 | |
| D | GLU45 | |
| D | GLU47 | |
| D | GLU50 | |
| D | GLU73 | |
| D | GLU126 | |
| D | GLU195 | |
| A | GLU73 | |
| D | GLU204 | |
| D | GLU367 | |
| D | GLU369 | |
| D | GLU406 | |
| D | GLU407 | |
| A | GLU126 | |
| A | GLU195 | |
| A | GLU204 | |
| A | GLU367 | |
| A | GLU369 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 28 |
| Details | MOD_RES: Aspartate methyl ester => ECO:0000305|PubMed:37385399 |
| Chain | Residue | Details |
| A | ASP72 | |
| B | ASP123 | |
| B | ASP203 | |
| B | ASP210 | |
| B | ASP370 | |
| B | ASP375 | |
| C | ASP72 | |
| C | ASP90 | |
| C | ASP123 | |
| C | ASP203 | |
| C | ASP210 | |
| A | ASP90 | |
| C | ASP370 | |
| C | ASP375 | |
| D | ASP72 | |
| D | ASP90 | |
| D | ASP123 | |
| D | ASP203 | |
| D | ASP210 | |
| D | ASP370 | |
| D | ASP375 | |
| A | ASP123 | |
| A | ASP203 | |
| A | ASP210 | |
| A | ASP370 | |
| A | ASP375 | |
| B | ASP72 | |
| B | ASP90 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000305|PubMed:37385399 |
| Chain | Residue | Details |
| A | LYS102 | |
| B | LYS102 | |
| C | LYS102 | |
| D | LYS102 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000305|PubMed:37385399 |
| Chain | Residue | Details |
| A | SER198 | |
| B | SER198 | |
| C | SER198 | |
| D | SER198 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphothreonine => ECO:0000305|PubMed:37385399 |
| Chain | Residue | Details |
| A | THR199 | |
| A | THR341 | |
| B | THR199 | |
| B | THR341 | |
| C | THR199 | |
| C | THR341 | |
| D | THR199 | |
| D | THR341 |
