3AO0
Crystal structure of ethanolamine ammonia-lyase from Escherichia coli complexed with CN-CBL and (S)-2-amino-1-propanol
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0008851 | molecular_function | ethanolamine ammonia-lyase activity |
| A | 0009350 | cellular_component | ethanolamine ammonia-lyase complex |
| A | 0016829 | molecular_function | lyase activity |
| A | 0031419 | molecular_function | cobalamin binding |
| A | 0031469 | cellular_component | bacterial microcompartment |
| A | 0031471 | cellular_component | ethanolamine degradation polyhedral organelle |
| A | 0046336 | biological_process | ethanolamine catabolic process |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0008851 | molecular_function | ethanolamine ammonia-lyase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0008851 | molecular_function | ethanolamine ammonia-lyase activity |
| C | 0009350 | cellular_component | ethanolamine ammonia-lyase complex |
| C | 0016829 | molecular_function | lyase activity |
| C | 0031419 | molecular_function | cobalamin binding |
| C | 0031469 | cellular_component | bacterial microcompartment |
| C | 0031471 | cellular_component | ethanolamine degradation polyhedral organelle |
| C | 0046336 | biological_process | ethanolamine catabolic process |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0008851 | molecular_function | ethanolamine ammonia-lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 2A1 A 602 |
| Chain | Residue |
| A | ARG160 |
| A | GLN162 |
| A | ASN193 |
| A | LEU225 |
| A | GLU287 |
| A | VAL326 |
| A | PHE329 |
| A | ASP362 |
| A | TYR404 |
| site_id | AC2 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE B12 B 601 |
| Chain | Residue |
| A | ASN193 |
| A | PRO194 |
| A | LEU225 |
| A | ALA226 |
| A | HIS227 |
| A | GLN246 |
| A | SER247 |
| A | GLU257 |
| A | PHE258 |
| A | SER295 |
| A | PHE329 |
| A | ILE330 |
| A | MET401 |
| A | LEU402 |
| A | HOH482 |
| A | HOH551 |
| A | HOH622 |
| B | ARG141 |
| B | ARG206 |
| B | VAL207 |
| B | LYS208 |
| B | GLY227 |
| B | GLU228 |
| B | ARG229 |
| B | TYR241 |
| B | GLU253 |
| B | ARG256 |
| B | CYS258 |
| B | SER260 |
| B | HOH298 |
| B | HOH300 |
| B | HOH361 |
| B | HOH470 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 2A1 C 602 |
| Chain | Residue |
| C | ARG160 |
| C | GLN162 |
| C | ASN193 |
| C | LEU225 |
| C | GLU287 |
| C | VAL326 |
| C | PHE329 |
| C | ASP362 |
| C | TYR404 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE B12 D 601 |
| Chain | Residue |
| C | ASN193 |
| C | PRO194 |
| C | LEU225 |
| C | ALA226 |
| C | HIS227 |
| C | GLN246 |
| C | SER247 |
| C | GLU257 |
| C | PHE258 |
| C | SER295 |
| C | ILE330 |
| C | MET401 |
| C | LEU402 |
| D | ARG141 |
| D | ARG206 |
| D | VAL207 |
| D | GLU228 |
| D | ARG229 |
| D | TYR241 |
| D | GLU253 |
| D | ARG256 |
| D | CYS258 |
| D | SER260 |
| D | HOH310 |
| D | HOH508 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00601, ECO:0000269|PubMed:20519496, ECO:0000269|PubMed:21142024, ECO:0007744|PDB:3ABO, ECO:0007744|PDB:3ABQ, ECO:0007744|PDB:3ABR, ECO:0007744|PDB:5YSN, ECO:0007744|PDB:5YSR |
| Chain | Residue | Details |
| B | VAL207 | |
| D | VAL207 | |
| A | ASP362 | |
| C | ARG160 | |
| C | GLU287 | |
| C | ASP362 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00601, ECO:0000269|PubMed:20519496, ECO:0000269|PubMed:21142024, ECO:0007744|PDB:3ABO, ECO:0007744|PDB:3ABQ, ECO:0007744|PDB:3ABR, ECO:0007744|PDB:3ANY, ECO:0007744|PDB:3AO0 |
| Chain | Residue | Details |
| B | GLU228 | |
| D | GLU228 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00601, ECO:0000269|PubMed:20519496, ECO:0000269|PubMed:21142024, ECO:0007744|PDB:3ABO, ECO:0007744|PDB:3ABR, ECO:0007744|PDB:3AO0, ECO:0007744|PDB:5YSN |
| Chain | Residue | Details |
| B | CYS258 | |
| D | CYS258 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00861, ECO:0000269|PubMed:20519496, ECO:0000269|PubMed:21142024, ECO:0007744|PDB:3ABO, ECO:0007744|PDB:3ABQ, ECO:0007744|PDB:3ANY, ECO:0007744|PDB:3AO0, ECO:0007744|PDB:5YSN |
| Chain | Residue | Details |
| A | GLN246 | |
| C | GLN246 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00861, ECO:0000305, ECO:0007744|PDB:3ABR, ECO:0007744|PDB:3ANY, ECO:0007744|PDB:3AO0 |
| Chain | Residue | Details |
| A | SER295 | |
| C | SER295 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00861, ECO:0000269|PubMed:20519496, ECO:0000269|PubMed:21142024, ECO:0007744|PDB:3ABO, ECO:0007744|PDB:3ABQ, ECO:0007744|PDB:3ANY, ECO:0007744|PDB:3AO0, ECO:0007744|PDB:5YSN, ECO:0007744|PDB:5YSR |
| Chain | Residue | Details |
| A | MET401 | |
| C | MET401 |
