1NMO
Structural genomics, protein ybgI, unknown function
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0010212 | biological_process | response to ionizing radiation |
| A | 0034214 | biological_process | protein hexamerization |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0060187 | cellular_component | cell pole |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0010212 | biological_process | response to ionizing radiation |
| B | 0034214 | biological_process | protein hexamerization |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0060187 | cellular_component | cell pole |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0010212 | biological_process | response to ionizing radiation |
| C | 0034214 | biological_process | protein hexamerization |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0060187 | cellular_component | cell pole |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0010212 | biological_process | response to ionizing radiation |
| D | 0034214 | biological_process | protein hexamerization |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0060187 | cellular_component | cell pole |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005829 | cellular_component | cytosol |
| E | 0010212 | biological_process | response to ionizing radiation |
| E | 0034214 | biological_process | protein hexamerization |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0060187 | cellular_component | cell pole |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005829 | cellular_component | cytosol |
| F | 0010212 | biological_process | response to ionizing radiation |
| F | 0034214 | biological_process | protein hexamerization |
| F | 0042802 | molecular_function | identical protein binding |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0060187 | cellular_component | cell pole |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE A 301 |
| Chain | Residue |
| A | HIS64 |
| A | HIS215 |
| A | GLU219 |
| A | FE302 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE A 302 |
| Chain | Residue |
| A | HIS63 |
| A | ASP101 |
| A | GLU219 |
| A | FE301 |
| A | HOH409 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE B 301 |
| Chain | Residue |
| B | HIS64 |
| B | HIS215 |
| B | GLU219 |
| B | FE302 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE B 302 |
| Chain | Residue |
| B | HIS63 |
| B | ASP101 |
| B | GLU219 |
| B | FE301 |
| B | HOH483 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE C 301 |
| Chain | Residue |
| C | HIS64 |
| C | HIS215 |
| C | GLU219 |
| C | FE302 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE C 302 |
| Chain | Residue |
| C | HIS63 |
| C | ASP101 |
| C | GLU219 |
| C | FE301 |
| C | HOH644 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE D 301 |
| Chain | Residue |
| D | HIS64 |
| D | HIS215 |
| D | GLU219 |
| D | FE302 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE D 302 |
| Chain | Residue |
| D | HIS63 |
| D | ASP101 |
| D | GLU219 |
| D | FE301 |
| D | HOH865 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE E 301 |
| Chain | Residue |
| E | HIS64 |
| E | HIS215 |
| E | GLU219 |
| E | FE302 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE E 302 |
| Chain | Residue |
| E | HIS63 |
| E | ASP101 |
| E | GLU219 |
| E | FE301 |
| E | HOH694 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE F 301 |
| Chain | Residue |
| F | HIS64 |
| F | HIS215 |
| F | GLU219 |
| F | FE302 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE F 302 |
| Chain | Residue |
| F | HIS63 |
| F | ASP101 |
| F | GLU219 |
| F | FE301 |
| F | HOH866 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14519207","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
