3ABO
Crystal structure of ethanolamine ammonia-lyase from Escherichia coli complexed with CN-Cbl and ethanolamine
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 ETA A 602 |
Chain | Residue |
A | ARG160 |
A | GLN162 |
A | ASN193 |
A | LEU225 |
A | GLU287 |
A | ASP362 |
A | MET392 |
A | LEU402 |
A | TYR404 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 1011 |
Chain | Residue |
A | GLY272 |
A | ALA273 |
A | GLY280 |
A | GLU281 |
A | ASN282 |
A | CYS283 |
A | HOH493 |
A | HOH529 |
C | ASN81 |
C | LYS115 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 1012 |
Chain | Residue |
A | LYS115 |
A | HOH606 |
A | HOH703 |
C | GLY272 |
C | ALA273 |
C | GLY280 |
C | GLU281 |
C | ASN282 |
C | CYS283 |
C | HOH522 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 1014 |
Chain | Residue |
A | ARG114 |
A | LYS145 |
A | ARG316 |
A | GLY356 |
A | HOH498 |
A | HOH758 |
site_id | AC5 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE B12 B 601 |
Chain | Residue |
A | ASN193 |
A | PRO194 |
A | LEU225 |
A | ALA226 |
A | HIS227 |
A | PHE245 |
A | GLN246 |
A | SER247 |
A | GLU257 |
A | PHE258 |
A | SER295 |
A | ILE330 |
A | MET401 |
A | LEU402 |
A | HOH513 |
A | HOH557 |
A | HOH653 |
B | ARG141 |
B | ARG206 |
B | VAL207 |
B | LYS208 |
B | GLU228 |
B | ARG229 |
B | TYR241 |
B | GLU253 |
B | ARG256 |
B | CYS258 |
B | SER260 |
B | HOH299 |
B | HOH300 |
B | HOH309 |
B | HOH311 |
B | HOH320 |
B | HOH617 |
B | HOH707 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ETA C 602 |
Chain | Residue |
C | ARG160 |
C | GLN162 |
C | ASN193 |
C | LEU225 |
C | GLU287 |
C | ASP362 |
C | MET392 |
C | LEU402 |
C | TYR404 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA C 1001 |
Chain | Residue |
A | HOH684 |
C | ASP338 |
C | ASP372 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL C 1013 |
Chain | Residue |
C | LYS145 |
C | ARG316 |
C | GLY356 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL C 1015 |
Chain | Residue |
C | ARG60 |
C | ASN61 |
C | GLU82 |
C | HOH568 |
site_id | BC1 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE B12 D 601 |
Chain | Residue |
C | MET401 |
C | LEU402 |
C | HOH496 |
C | HOH727 |
D | ARG141 |
D | ARG206 |
D | VAL207 |
D | GLY227 |
D | GLU228 |
D | ARG229 |
D | TYR241 |
D | GLU253 |
D | ARG256 |
D | CYS258 |
D | SER260 |
D | ASN261 |
D | HOH371 |
D | HOH491 |
D | HOH557 |
D | HOH618 |
C | PRO194 |
C | LEU225 |
C | ALA226 |
C | HIS227 |
C | GLN246 |
C | SER247 |
C | GLU257 |
C | PHE258 |
C | SER295 |
C | ILE330 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA D 1002 |
Chain | Residue |
C | GLU179 |
D | ARG77 |
D | THR80 |
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 |