4M1I
X-ray crystal structure of Chlamydia trachomatis Mn(II)Fe(II)-NrdB
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| A | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| B | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| C | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| D | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN A 401 |
| Chain | Residue |
| A | GLU89 |
| A | GLU120 |
| A | HIS123 |
| A | GLU227 |
| A | FE402 |
| A | HOH501 |
| A | HOH502 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 402 |
| Chain | Residue |
| A | GLU227 |
| A | HIS230 |
| A | MN401 |
| A | HOH501 |
| A | GLU120 |
| A | GLU193 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE P6G A 403 |
| Chain | Residue |
| A | GLN179 |
| A | GLU180 |
| A | LYS183 |
| A | GLU256 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE B 401 |
| Chain | Residue |
| B | GLU120 |
| B | GLU193 |
| B | GLU227 |
| B | HIS230 |
| B | MN402 |
| B | HOH501 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN B 402 |
| Chain | Residue |
| B | GLU89 |
| B | GLU120 |
| B | HIS123 |
| B | GLU227 |
| B | FE401 |
| B | HOH501 |
| B | HOH502 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACY B 403 |
| Chain | Residue |
| B | VAL13 |
| B | LYS18 |
| B | VAL26 |
| B | ASP27 |
| B | GLN30 |
| B | PRO107 |
| B | HOH530 |
| B | HOH752 |
| B | HOH753 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE C 401 |
| Chain | Residue |
| C | GLU120 |
| C | GLU193 |
| C | GLU227 |
| C | HIS230 |
| C | MN402 |
| C | HOH501 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN C 402 |
| Chain | Residue |
| C | GLU89 |
| C | GLU120 |
| C | HIS123 |
| C | GLU227 |
| C | FE401 |
| C | HOH501 |
| C | HOH502 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE P6G C 403 |
| Chain | Residue |
| C | GLN179 |
| C | GLU180 |
| C | LYS183 |
| C | GLU256 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE D 401 |
| Chain | Residue |
| D | GLU120 |
| D | GLU193 |
| D | GLU227 |
| D | HIS230 |
| D | MN402 |
| D | HOH501 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN D 402 |
| Chain | Residue |
| D | GLU89 |
| D | GLU120 |
| D | HIS123 |
| D | GLU227 |
| D | FE401 |
| D | HOH501 |
| D | HOH502 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
