2JH3
The crystal structure of DR2241 from Deinococcus radiodurans at 1.9 A resolution reveals a multi-domain protein with structural similarity to chelatases but also with two additional novel domains
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019354 | biological_process | siroheme biosynthetic process |
| A | 0051266 | molecular_function | sirohydrochlorin ferrochelatase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019354 | biological_process | siroheme biosynthetic process |
| B | 0051266 | molecular_function | sirohydrochlorin ferrochelatase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0019354 | biological_process | siroheme biosynthetic process |
| C | 0051266 | molecular_function | sirohydrochlorin ferrochelatase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0019354 | biological_process | siroheme biosynthetic process |
| D | 0051266 | molecular_function | sirohydrochlorin ferrochelatase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SF4 A 650 |
| Chain | Residue |
| A | TRP346 |
| A | CYS420 |
| A | CYS423 |
| A | CYS448 |
| A | CYS452 |
| A | LEU455 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SF4 B 650 |
| Chain | Residue |
| B | CYS448 |
| B | CYS452 |
| B | TRP346 |
| B | CYS420 |
| B | CYS423 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SF4 C 650 |
| Chain | Residue |
| C | TRP346 |
| C | CYS420 |
| C | CYS423 |
| C | CYS448 |
| C | CYS452 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SF4 D 650 |
| Chain | Residue |
| D | TRP346 |
| D | CYS420 |
| D | CYS423 |
| D | CYS448 |
| D | CYS452 |
Functional Information from PROSITE/UniProt
| site_id | PS00178 |
| Number of Residues | 11 |
| Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Pq.APpLHVGGP |
| Chain | Residue | Details |
| A | PRO234-PRO244 |
