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 |
A | SER42 | |
A | GLN162 | |
B | SER42 | |
B | GLN162 | |
C | SER42 | |
C | GLN162 | |
D | SER42 | |
D | 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 |