4AC8
R2-like ligand binding Mn-Fe oxidase from M. tuberculosis with an organized C-terminal helix
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0030145 | molecular_function | manganese ion binding |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0030145 | molecular_function | manganese ion binding |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 500 |
| Chain | Residue |
| A | GLU101 |
| A | GLU167 |
| A | GLU202 |
| A | HIS205 |
| A | MN501 |
| A | MYR600 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 501 |
| Chain | Residue |
| A | GLU202 |
| A | FE500 |
| A | MYR600 |
| A | GLU68 |
| A | GLU101 |
| A | HIS104 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE MYR A 600 |
| Chain | Residue |
| A | TYR56 |
| A | PHE64 |
| A | GLU68 |
| A | GLU101 |
| A | GLU167 |
| A | LEU170 |
| A | GLU202 |
| A | PHE246 |
| A | PHE262 |
| A | FE500 |
| A | MN501 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE B 500 |
| Chain | Residue |
| B | GLU101 |
| B | GLU167 |
| B | GLU202 |
| B | HIS205 |
| B | MN501 |
| B | MYR600 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 501 |
| Chain | Residue |
| B | GLU68 |
| B | GLU101 |
| B | HIS104 |
| B | GLU202 |
| B | FE500 |
| B | MYR600 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE MYR B 600 |
| Chain | Residue |
| B | TYR56 |
| B | GLN63 |
| B | GLU68 |
| B | VAL71 |
| B | GLU101 |
| B | PHE135 |
| B | GLU167 |
| B | ALA171 |
| B | GLU202 |
| B | PHE246 |
| B | FE500 |
| B | MN501 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE C 500 |
| Chain | Residue |
| C | GLU101 |
| C | GLU167 |
| C | GLU202 |
| C | HIS205 |
| C | MN501 |
| C | MYR600 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN C 501 |
| Chain | Residue |
| C | GLU68 |
| C | GLU101 |
| C | HIS104 |
| C | GLU202 |
| C | FE500 |
| C | MYR600 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MYR C 600 |
| Chain | Residue |
| C | TYR56 |
| C | PHE64 |
| C | GLU68 |
| C | GLU101 |
| C | GLU167 |
| C | GLU202 |
| C | FE500 |
| C | MN501 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE D 500 |
| Chain | Residue |
| D | GLU101 |
| D | GLU167 |
| D | GLU202 |
| D | HIS205 |
| D | MN501 |
| D | MYR600 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN D 501 |
| Chain | Residue |
| D | GLU68 |
| D | GLU101 |
| D | HIS104 |
| D | GLU202 |
| D | FE500 |
| D | MYR600 |
| site_id | BC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE MYR D 600 |
| Chain | Residue |
| D | TYR56 |
| D | LEU60 |
| D | PHE64 |
| D | GLU68 |
| D | GLU101 |
| D | PHE135 |
| D | GLU167 |
| D | LEU170 |
| D | GLU202 |
| D | FE500 |
| D | MN501 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 1311 |
| Chain | Residue |
| B | ASP268 |
| B | GLU304 |
| B | HOH2023 |
| B | HOH2025 |
| C | ASP268 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 1313 |
| Chain | Residue |
| D | ASP268 |
| A | ASP268 |
| A | GLU304 |
| A | HOH2030 |
| A | HOH2032 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 1314 |
| Chain | Residue |
| A | GLU138 |
| A | HOH2018 |
| B | GLU243 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19321420, ECO:0000269|PubMed:22976985, ECO:0007744|PDB:3EE4, ECO:0007744|PDB:4AC8 |
| Chain | Residue | Details |
| B | HIS104 | |
| B | GLU167 | |
| B | GLU202 | |
| B | HIS205 | |
| C | GLU68 | |
| C | GLU101 | |
| C | HIS104 | |
| C | GLU167 | |
| C | GLU202 | |
| C | HIS205 | |
| D | GLU68 | |
| D | GLU101 | |
| D | HIS104 | |
| D | GLU167 | |
| D | GLU202 | |
| D | HIS205 | |
| A | GLU68 | |
| A | GLU101 | |
| A | HIS104 | |
| A | GLU167 | |
| A | GLU202 | |
| A | HIS205 | |
| B | GLU68 | |
| B | GLU101 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | CROSSLNK: 3-(O4'-tyrosyl)-valine (Val-Tyr) => ECO:0000269|PubMed:19321420, ECO:0000269|PubMed:22976985 |
| Chain | Residue | Details |
| C | VAL71 | |
| C | TYR162 | |
| D | VAL71 | |
| D | TYR162 | |
| A | VAL71 | |
| A | TYR162 | |
| B | VAL71 | |
| B | TYR162 |
