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 | 0006281 | biological_process | DNA repair |
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 | 0006281 | biological_process | DNA repair |
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 | 0006281 | biological_process | DNA repair |
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 | 0006281 | biological_process | DNA repair |
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 | 0006281 | biological_process | DNA repair |
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 | 0006281 | biological_process | DNA repair |
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: BINDING => ECO:0000269|PubMed:14519207 |
Chain | Residue | Details |
A | HIS63 | |
B | GLU219 | |
C | HIS63 | |
C | HIS64 | |
C | ASP101 | |
C | HIS215 | |
C | GLU219 | |
D | HIS63 | |
D | HIS64 | |
D | ASP101 | |
D | HIS215 | |
A | HIS64 | |
D | GLU219 | |
E | HIS63 | |
E | HIS64 | |
E | ASP101 | |
E | HIS215 | |
E | GLU219 | |
F | HIS63 | |
F | HIS64 | |
F | ASP101 | |
F | HIS215 | |
A | ASP101 | |
F | GLU219 | |
A | HIS215 | |
A | GLU219 | |
B | HIS63 | |
B | HIS64 | |
B | ASP101 | |
B | HIS215 |