3ABR
Crystal structure of ethanolamine ammonia-lyase from Escherichia coli complexed with CN-Cbl (substrate-free form)
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 |
| B | 0009350 | cellular_component | ethanolamine ammonia-lyase complex |
| B | 0016829 | molecular_function | lyase activity |
| B | 0031419 | molecular_function | cobalamin binding |
| B | 0031469 | cellular_component | bacterial microcompartment |
| B | 0031471 | cellular_component | ethanolamine degradation polyhedral organelle |
| B | 0046336 | biological_process | ethanolamine catabolic process |
| 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 |
| D | 0009350 | cellular_component | ethanolamine ammonia-lyase complex |
| D | 0016829 | molecular_function | lyase activity |
| D | 0031419 | molecular_function | cobalamin binding |
| D | 0031469 | cellular_component | bacterial microcompartment |
| D | 0031471 | cellular_component | ethanolamine degradation polyhedral organelle |
| D | 0046336 | biological_process | ethanolamine catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 2001 |
| Chain | Residue |
| A | GLY272 |
| A | ALA273 |
| A | ILE278 |
| A | GLY280 |
| A | GLU281 |
| A | ASN282 |
| A | CYS283 |
| A | HOH976 |
| C | LYS115 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 2002 |
| Chain | Residue |
| A | LYS115 |
| C | GLY272 |
| C | ALA273 |
| C | GLY280 |
| C | GLU281 |
| C | ASN282 |
| C | CYS283 |
| C | HOH558 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 2006 |
| Chain | Residue |
| A | ASN148 |
| A | ARG277 |
| A | HOH466 |
| A | HOH711 |
| C | GLN87 |
| C | PHE112 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 3001 |
| Chain | Residue |
| A | SER295 |
| A | TYR334 |
| B | PRO137 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 3004 |
| Chain | Residue |
| A | ILE235 |
| A | GLY238 |
| A | ALA239 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 3005 |
| Chain | Residue |
| A | ASP398 |
| B | VAL75 |
| B | HOH348 |
| site_id | AC7 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE B12 B 601 |
| Chain | Residue |
| A | ASN193 |
| A | PRO194 |
| A | SER247 |
| A | GLU257 |
| A | PHE258 |
| A | SER295 |
| A | PHE329 |
| A | ILE330 |
| A | MET401 |
| A | LEU402 |
| A | HOH518 |
| A | HOH524 |
| B | ARG141 |
| B | ARG206 |
| B | VAL207 |
| B | LYS208 |
| B | GLU228 |
| B | ARG229 |
| B | TYR241 |
| B | GLU253 |
| B | ARG256 |
| B | CYS258 |
| B | SER260 |
| B | ASN261 |
| B | HOH307 |
| B | HOH313 |
| B | HOH320 |
| B | HOH322 |
| B | HOH533 |
| B | HOH872 |
| B | HOH895 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 3002 |
| Chain | Residue |
| B | LEU96 |
| B | SER100 |
| B | HOH913 |
| C | VAL45 |
| C | HOH466 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 2003 |
| Chain | Residue |
| C | ILE144 |
| C | LYS145 |
| C | LYS146 |
| C | THR150 |
| C | HOH665 |
| C | HOH898 |
| C | HOH936 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 2004 |
| Chain | Residue |
| A | HOH590 |
| A | HOH616 |
| C | VAL143 |
| C | LYS145 |
| C | ARG316 |
| C | GLY356 |
| C | HOH469 |
| C | HOH795 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL C 2005 |
| Chain | Residue |
| C | ARG60 |
| C | ASN61 |
| C | HOH943 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE NA C 3007 |
| Chain | Residue |
| C | ASP69 |
| site_id | BC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE B12 D 601 |
| Chain | Residue |
| D | TYR133 |
| D | ARG141 |
| D | ARG206 |
| D | VAL207 |
| D | GLU228 |
| D | ARG229 |
| D | TYR241 |
| D | GLU253 |
| D | ARG256 |
| D | CYS258 |
| D | SER260 |
| D | HOH309 |
| D | HOH310 |
| D | HOH315 |
| D | HOH357 |
| D | HOH568 |
| D | HOH735 |
| C | PRO194 |
| C | LEU225 |
| C | PHE245 |
| C | SER247 |
| C | GLU257 |
| C | PHE258 |
| C | SER295 |
| C | PHE329 |
| C | ILE330 |
| C | MET401 |
| C | LEU402 |
| C | HOH492 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA D 3003 |
| Chain | Residue |
| D | SER170 |
| D | GLU228 |
| D | SER235 |
| D | SER237 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA D 3006 |
| Chain | Residue |
| D | SER260 |
| D | ASN261 |
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 |
